> top > docs > PubMed:1321144 > annotations

PubMed:1321144 JSONTXT

Annnotations TAB JSON ListView MergeView

GlyCosmos6-Glycan-Motif-Image

Id Subject Object Predicate Lexical cue image
T1 682-693 Glycan_Motif denotes sialic acid https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY

sentences

Id Subject Object Predicate Lexical cue
T1 0-92 Sentence denotes Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex.
T2 93-146 Sentence denotes Structural basis for cooperative lectin-cell binding.
T3 147-532 Sentence denotes The crystal structure of wheat germ agglutinin isolectin 1 (WGA1) complexed with a tryptic sialoglycopeptide fragment (T-5) from its erythrocyte receptor glycophorin A, which contains the O-linked tetrasaccharide NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc) Gal-NAc-alpha 1-O-Thr, has been determined by molecular replacement techniques and refined at 2.0-A resolution (R = 18.1%).
T4 533-753 Sentence denotes The structure reveals that association between WGA1 dimers, composed of two identical four-domain (A-D) monomers, and T-5 is asymmetric and involves sialic acid binding at three nonequivalent aromatic residue-rich sites.
T5 754-797 Sentence denotes Two independent binding modes are observed.
T6 798-949 Sentence denotes In the dominant ("major") binding mode, the two highest affinity sites are utilized to cross-link neighboring crystallographically related WGA1 dimers.
T7 950-1182 Sentence denotes The branched tetrasaccharide has an extended rigid conformation, and its terminal alpha 2,6-NeuNAc and alpha 2,3-NeuNAc residues occupy specificity sites in domains B1 (monomer 1) and C2 (monomer 2) on opposing dimers, respectively.
T8 1183-1294 Sentence denotes This asymmetric selection of binding sites leads to infinite open-ended arrays of interlinked lectin molecules.
T9 1295-1455 Sentence denotes In the subsidiary "minor" binding mode, only the terminal alpha 2,6-NeuNAc, anchored to the aromatic residue-rich binding site in domain A2, is clearly visible.
T10 1456-1499 Sentence denotes The remaining portion of T-5 is disordered.
T11 1500-1677 Sentence denotes This structure presents the first evidence for NeuNAc binding in the aromatic residue-rich sites of domains A and C and suggests a preference of WGA for alpha 2,6-linked NeuNAc.
T12 1678-1913 Sentence denotes Moreover, the unusual asymmetric WGA1-tetrasaccharide association, involving domain binding sites that differ in their binding affinities for NeuNAc, offers explanations for the widely observed cooperative cell binding behavior of WGA.
T1 0-92 Sentence denotes Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex.
T2 93-146 Sentence denotes Structural basis for cooperative lectin-cell binding.
T3 147-532 Sentence denotes The crystal structure of wheat germ agglutinin isolectin 1 (WGA1) complexed with a tryptic sialoglycopeptide fragment (T-5) from its erythrocyte receptor glycophorin A, which contains the O-linked tetrasaccharide NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc) Gal-NAc-alpha 1-O-Thr, has been determined by molecular replacement techniques and refined at 2.0-A resolution (R = 18.1%).
T4 533-753 Sentence denotes The structure reveals that association between WGA1 dimers, composed of two identical four-domain (A-D) monomers, and T-5 is asymmetric and involves sialic acid binding at three nonequivalent aromatic residue-rich sites.
T5 754-797 Sentence denotes Two independent binding modes are observed.
T6 798-949 Sentence denotes In the dominant ("major") binding mode, the two highest affinity sites are utilized to cross-link neighboring crystallographically related WGA1 dimers.
T7 950-1182 Sentence denotes The branched tetrasaccharide has an extended rigid conformation, and its terminal alpha 2,6-NeuNAc and alpha 2,3-NeuNAc residues occupy specificity sites in domains B1 (monomer 1) and C2 (monomer 2) on opposing dimers, respectively.
T8 1183-1294 Sentence denotes This asymmetric selection of binding sites leads to infinite open-ended arrays of interlinked lectin molecules.
T9 1295-1455 Sentence denotes In the subsidiary "minor" binding mode, only the terminal alpha 2,6-NeuNAc, anchored to the aromatic residue-rich binding site in domain A2, is clearly visible.
T10 1456-1499 Sentence denotes The remaining portion of T-5 is disordered.
T11 1500-1677 Sentence denotes This structure presents the first evidence for NeuNAc binding in the aromatic residue-rich sites of domains A and C and suggests a preference of WGA for alpha 2,6-linked NeuNAc.
T12 1678-1913 Sentence denotes Moreover, the unusual asymmetric WGA1-tetrasaccharide association, involving domain binding sites that differ in their binding affinities for NeuNAc, offers explanations for the widely observed cooperative cell binding behavior of WGA.

GlyCosmos6-Glycan-Motif-Structure

Id Subject Object Predicate Lexical cue
T1 682-693 https://glytoucan.org/Structures/Glycans/G81533KY denotes sialic acid

Glycan-GlyCosmos

Id Subject Object Predicate Lexical cue image
T1 360-366 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T2 401-407 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T3 409-416 Glycan denotes Gal-NAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL
T4 1042-1048 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T5 1063-1069 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T6 1363-1369 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T7 1547-1553 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T8 1670-1676 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T9 1820-1826 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR

GlyCosmos15-NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 23-28 OrganismTaxon denotes wheat 4565
T2 172-177 OrganismTaxon denotes wheat 4565

GlyCosmos15-CL

Id Subject Object Predicate Lexical cue cl_id
T1 280-291 Cell denotes erythrocyte http://purl.obolibrary.org/obo/CL:0000232

GlyCosmos15-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 280-291 Body_part denotes erythrocyte http://purl.obolibrary.org/obo/CL_0000232

sentences

Id Subject Object Predicate Lexical cue
T1 0-92 Sentence denotes Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex.
T2 93-146 Sentence denotes Structural basis for cooperative lectin-cell binding.
T3 147-532 Sentence denotes The crystal structure of wheat germ agglutinin isolectin 1 (WGA1) complexed with a tryptic sialoglycopeptide fragment (T-5) from its erythrocyte receptor glycophorin A, which contains the O-linked tetrasaccharide NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc) Gal-NAc-alpha 1-O-Thr, has been determined by molecular replacement techniques and refined at 2.0-A resolution (R = 18.1%).
T4 533-753 Sentence denotes The structure reveals that association between WGA1 dimers, composed of two identical four-domain (A-D) monomers, and T-5 is asymmetric and involves sialic acid binding at three nonequivalent aromatic residue-rich sites.
T5 754-797 Sentence denotes Two independent binding modes are observed.
T6 798-949 Sentence denotes In the dominant ("major") binding mode, the two highest affinity sites are utilized to cross-link neighboring crystallographically related WGA1 dimers.
T7 950-1182 Sentence denotes The branched tetrasaccharide has an extended rigid conformation, and its terminal alpha 2,6-NeuNAc and alpha 2,3-NeuNAc residues occupy specificity sites in domains B1 (monomer 1) and C2 (monomer 2) on opposing dimers, respectively.
T8 1183-1294 Sentence denotes This asymmetric selection of binding sites leads to infinite open-ended arrays of interlinked lectin molecules.
T9 1295-1455 Sentence denotes In the subsidiary "minor" binding mode, only the terminal alpha 2,6-NeuNAc, anchored to the aromatic residue-rich binding site in domain A2, is clearly visible.
T10 1456-1499 Sentence denotes The remaining portion of T-5 is disordered.
T11 1500-1677 Sentence denotes This structure presents the first evidence for NeuNAc binding in the aromatic residue-rich sites of domains A and C and suggests a preference of WGA for alpha 2,6-linked NeuNAc.
T12 1678-1913 Sentence denotes Moreover, the unusual asymmetric WGA1-tetrasaccharide association, involving domain binding sites that differ in their binding affinities for NeuNAc, offers explanations for the widely observed cooperative cell binding behavior of WGA.
T1 0-92 Sentence denotes Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex.
T2 93-146 Sentence denotes Structural basis for cooperative lectin-cell binding.
T3 147-532 Sentence denotes The crystal structure of wheat germ agglutinin isolectin 1 (WGA1) complexed with a tryptic sialoglycopeptide fragment (T-5) from its erythrocyte receptor glycophorin A, which contains the O-linked tetrasaccharide NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc) Gal-NAc-alpha 1-O-Thr, has been determined by molecular replacement techniques and refined at 2.0-A resolution (R = 18.1%).
T4 533-753 Sentence denotes The structure reveals that association between WGA1 dimers, composed of two identical four-domain (A-D) monomers, and T-5 is asymmetric and involves sialic acid binding at three nonequivalent aromatic residue-rich sites.
T5 754-797 Sentence denotes Two independent binding modes are observed.
T6 798-949 Sentence denotes In the dominant ("major") binding mode, the two highest affinity sites are utilized to cross-link neighboring crystallographically related WGA1 dimers.
T7 950-1182 Sentence denotes The branched tetrasaccharide has an extended rigid conformation, and its terminal alpha 2,6-NeuNAc and alpha 2,3-NeuNAc residues occupy specificity sites in domains B1 (monomer 1) and C2 (monomer 2) on opposing dimers, respectively.
T8 1183-1294 Sentence denotes This asymmetric selection of binding sites leads to infinite open-ended arrays of interlinked lectin molecules.
T9 1295-1455 Sentence denotes In the subsidiary "minor" binding mode, only the terminal alpha 2,6-NeuNAc, anchored to the aromatic residue-rich binding site in domain A2, is clearly visible.
T10 1456-1499 Sentence denotes The remaining portion of T-5 is disordered.
T11 1500-1677 Sentence denotes This structure presents the first evidence for NeuNAc binding in the aromatic residue-rich sites of domains A and C and suggests a preference of WGA for alpha 2,6-linked NeuNAc.
T12 1678-1913 Sentence denotes Moreover, the unusual asymmetric WGA1-tetrasaccharide association, involving domain binding sites that differ in their binding affinities for NeuNAc, offers explanations for the widely observed cooperative cell binding behavior of WGA.

GlyCosmos15-Sentences

Id Subject Object Predicate Lexical cue
T1 0-92 Sentence denotes Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex.
T2 93-146 Sentence denotes Structural basis for cooperative lectin-cell binding.
T3 147-532 Sentence denotes The crystal structure of wheat germ agglutinin isolectin 1 (WGA1) complexed with a tryptic sialoglycopeptide fragment (T-5) from its erythrocyte receptor glycophorin A, which contains the O-linked tetrasaccharide NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc) Gal-NAc-alpha 1-O-Thr, has been determined by molecular replacement techniques and refined at 2.0-A resolution (R = 18.1%).
T4 533-753 Sentence denotes The structure reveals that association between WGA1 dimers, composed of two identical four-domain (A-D) monomers, and T-5 is asymmetric and involves sialic acid binding at three nonequivalent aromatic residue-rich sites.
T5 754-797 Sentence denotes Two independent binding modes are observed.
T6 798-949 Sentence denotes In the dominant ("major") binding mode, the two highest affinity sites are utilized to cross-link neighboring crystallographically related WGA1 dimers.
T7 950-1182 Sentence denotes The branched tetrasaccharide has an extended rigid conformation, and its terminal alpha 2,6-NeuNAc and alpha 2,3-NeuNAc residues occupy specificity sites in domains B1 (monomer 1) and C2 (monomer 2) on opposing dimers, respectively.
T8 1183-1294 Sentence denotes This asymmetric selection of binding sites leads to infinite open-ended arrays of interlinked lectin molecules.
T9 1295-1455 Sentence denotes In the subsidiary "minor" binding mode, only the terminal alpha 2,6-NeuNAc, anchored to the aromatic residue-rich binding site in domain A2, is clearly visible.
T10 1456-1499 Sentence denotes The remaining portion of T-5 is disordered.
T11 1500-1677 Sentence denotes This structure presents the first evidence for NeuNAc binding in the aromatic residue-rich sites of domains A and C and suggests a preference of WGA for alpha 2,6-linked NeuNAc.
T12 1678-1913 Sentence denotes Moreover, the unusual asymmetric WGA1-tetrasaccharide association, involving domain binding sites that differ in their binding affinities for NeuNAc, offers explanations for the widely observed cooperative cell binding behavior of WGA.

GlyCosmos15-Lectin-Jamboree

Id Subject Object Predicate Lexical cue glycosmos_id
T1 1645-1648 Lectin denotes WGA GL_003502
T2 1909-1912 Lectin denotes WGA GL_003502

Lectin-Jamboree-small

Id Subject Object Predicate Lexical cue glycosmos_id
T1 1645-1648 Lectin denotes WGA GL_000044
T2 1909-1912 Lectin denotes WGA GL_000044

Lectin-Jamboree-Sentence

Id Subject Object Predicate Lexical cue
T1 0-92 Sentence denotes Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex.
T2 93-146 Sentence denotes Structural basis for cooperative lectin-cell binding.
T3 147-532 Sentence denotes The crystal structure of wheat germ agglutinin isolectin 1 (WGA1) complexed with a tryptic sialoglycopeptide fragment (T-5) from its erythrocyte receptor glycophorin A, which contains the O-linked tetrasaccharide NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc) Gal-NAc-alpha 1-O-Thr, has been determined by molecular replacement techniques and refined at 2.0-A resolution (R = 18.1%).
T4 533-753 Sentence denotes The structure reveals that association between WGA1 dimers, composed of two identical four-domain (A-D) monomers, and T-5 is asymmetric and involves sialic acid binding at three nonequivalent aromatic residue-rich sites.
T5 754-797 Sentence denotes Two independent binding modes are observed.
T6 798-949 Sentence denotes In the dominant ("major") binding mode, the two highest affinity sites are utilized to cross-link neighboring crystallographically related WGA1 dimers.
T7 950-1182 Sentence denotes The branched tetrasaccharide has an extended rigid conformation, and its terminal alpha 2,6-NeuNAc and alpha 2,3-NeuNAc residues occupy specificity sites in domains B1 (monomer 1) and C2 (monomer 2) on opposing dimers, respectively.
T8 1183-1294 Sentence denotes This asymmetric selection of binding sites leads to infinite open-ended arrays of interlinked lectin molecules.
T9 1295-1455 Sentence denotes In the subsidiary "minor" binding mode, only the terminal alpha 2,6-NeuNAc, anchored to the aromatic residue-rich binding site in domain A2, is clearly visible.
T10 1456-1499 Sentence denotes The remaining portion of T-5 is disordered.
T11 1500-1677 Sentence denotes This structure presents the first evidence for NeuNAc binding in the aromatic residue-rich sites of domains A and C and suggests a preference of WGA for alpha 2,6-linked NeuNAc.
T12 1678-1913 Sentence denotes Moreover, the unusual asymmetric WGA1-tetrasaccharide association, involving domain binding sites that differ in their binding affinities for NeuNAc, offers explanations for the widely observed cooperative cell binding behavior of WGA.

GlyCosmos15-FMA

Id Subject Object Predicate Lexical cue db_id
T1 280-291 Body_part denotes erythrocyte FMA:62845

GlyCosmos15-Glycan

Id Subject Object Predicate Lexical cue image
T1 360-366 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T2 401-407 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T3 409-416 Glycan denotes Gal-NAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL
T4 1042-1048 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T5 1063-1069 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T6 1363-1369 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T7 1547-1553 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T8 1670-1676 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR
T9 1820-1826 Glycan denotes NeuNAc https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 23-28 OrganismTaxon denotes wheat 4565
T2 172-177 OrganismTaxon denotes wheat 4565

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 280-291 Body_part denotes erythrocyte http://purl.obolibrary.org/obo/CL_0000232

CL-cell

Id Subject Object Predicate Lexical cue cl_id
T1 280-291 Cell denotes erythrocyte http://purl.obolibrary.org/obo/CL:0000232