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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-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

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_003502
T2 1909-1912 Lectin denotes WGA GL_003502

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.

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