PubMed:12634320 JSON TXT

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Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":666,"end":675},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":666,"end":675},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":832,"end":841},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T4","span":{"begin":832,"end":841},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T5","span":{"begin":956,"end":965},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T6","span":{"begin":956,"end":965},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T7","span":{"begin":1077,"end":1086},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T8","span":{"begin":1077,"end":1086},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T9","span":{"begin":1204,"end":1213},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T10","span":{"begin":1204,"end":1213},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T11","span":{"begin":1709,"end":1718},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T12","span":{"begin":1709,"end":1718},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":666,"end":675},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":832,"end":841},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":956,"end":965},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1077,"end":1086},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":1204,"end":1213},"obj":"Glycan_Motif"},{"id":"T11","span":{"begin":1709,"end":1718},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A8","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A10","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A11","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A12","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":666,"end":675},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":666,"end":675},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":832,"end":841},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T4","span":{"begin":832,"end":841},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T5","span":{"begin":956,"end":965},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T6","span":{"begin":956,"end":965},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T7","span":{"begin":1077,"end":1086},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T8","span":{"begin":1077,"end":1086},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T9","span":{"begin":1204,"end":1213},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T10","span":{"begin":1204,"end":1213},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T11","span":{"begin":1709,"end":1718},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T12","span":{"begin":1709,"end":1718},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

sentences

GlycoBiology-FMA

uniprot-human

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":45,"end":48},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T2","span":{"begin":191,"end":194},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T3","span":{"begin":270,"end":273},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T4","span":{"begin":316,"end":319},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T5","span":{"begin":1458,"end":1461},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T6","span":{"begin":1505,"end":1508},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T7","span":{"begin":1620,"end":1623},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T8","span":{"begin":1690,"end":1693},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T9","span":{"begin":1776,"end":1779},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T10","span":{"begin":1838,"end":1841},"obj":"http://www.uniprot.org/uniprot/P97315"},{"id":"T11","span":{"begin":167,"end":185},"obj":"http://www.uniprot.org/uniprot/P14847"},{"id":"T12","span":{"begin":420,"end":433},"obj":"http://www.uniprot.org/uniprot/P07724"},{"id":"T13","span":{"begin":549,"end":551},"obj":"http://www.uniprot.org/uniprot/Q9R0M4"},{"id":"T14","span":{"begin":590,"end":592},"obj":"http://www.uniprot.org/uniprot/Q9R0M4"},{"id":"T15","span":{"begin":755,"end":757},"obj":"http://www.uniprot.org/uniprot/Q9R0M4"},{"id":"T16","span":{"begin":1269,"end":1271},"obj":"http://www.uniprot.org/uniprot/Q9R0M4"},{"id":"T17","span":{"begin":1444,"end":1446},"obj":"http://www.uniprot.org/uniprot/Q9R0M4"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":1179,"end":1184},"obj":"http://purl.bioontology.org/ontology/STY/T096"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":1532,"end":1534},"obj":"http://purl.obolibrary.org/obo/GO_0004306"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

GO-MF

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":420,"end":425},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":0,"end":12},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":35,"end":40},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":157,"end":162},"obj":"http://edamontology.org/topic_2815"},{"id":"T4","span":{"begin":178,"end":185},"obj":"http://edamontology.org/topic_0078"},{"id":"T5","span":{"begin":237,"end":252},"obj":"http://edamontology.org/topic_3300"},{"id":"T6","span":{"begin":280,"end":287},"obj":"http://edamontology.org/topic_3678"},{"id":"T7","span":{"begin":308,"end":315},"obj":"http://edamontology.org/topic_0632"},{"id":"T8","span":{"begin":878,"end":890},"obj":"http://edamontology.org/topic_0152"},{"id":"T9","span":{"begin":1343,"end":1351},"obj":"http://edamontology.org/topic_2269"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":0,"end":31},"obj":"http://edamontology.org/data_3425"},{"id":"T2","span":{"begin":136,"end":141},"obj":"http://edamontology.org/data_2100"},{"id":"T3","span":{"begin":178,"end":185},"obj":"http://edamontology.org/format_1208"},{"id":"T4","span":{"begin":178,"end":185},"obj":"http://edamontology.org/data_1467"},{"id":"T5","span":{"begin":473,"end":481},"obj":"http://edamontology.org/data_1756"},{"id":"T6","span":{"begin":492,"end":502},"obj":"http://edamontology.org/data_0883"},{"id":"T7","span":{"begin":576,"end":584},"obj":"http://edamontology.org/data_1756"},{"id":"T8","span":{"begin":744,"end":746},"obj":"http://edamontology.org/format_1997"},{"id":"T9","span":{"begin":787,"end":789},"obj":"http://edamontology.org/format_1997"},{"id":"T10","span":{"begin":821,"end":823},"obj":"http://edamontology.org/format_1997"},{"id":"T11","span":{"begin":1033,"end":1047},"obj":"http://edamontology.org/data_2746"},{"id":"T12","span":{"begin":1048,"end":1061},"obj":"http://edamontology.org/data_2726"},{"id":"T13","span":{"begin":1521,"end":1526},"obj":"http://edamontology.org/operation_3454"},{"id":"T14","span":{"begin":1521,"end":1526},"obj":"http://edamontology.org/data_2336"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":1535,"end":1537},"obj":"https://acgg.asia/db/lfdb/LfDB0344"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":371,"end":378},"obj":"id"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":1436,"end":1443},"obj":"id"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

GlyTouCan-IUPAC

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":420,"end":425},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":35,"end":40},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":157,"end":162},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":413,"end":419},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9913"}],"text":"Carbohydrate-binding properties of human neo-CRP and its relationship to phosphorylcholine-binding site.\nBinding characteristics of two types of ligands for human neo-C-reactive protein (neo-CRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on a polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin derivatives that contain on average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather nonspecific: the binding site prefers galactose configuration, but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neo-CRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem., 277, 225-232], whereas binding of sugar phosphates by neo-CRP shows considerably less stringent requirements compared to native CRP. For instance, galactose-alpha1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neo-CRP assay."}