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1JYI

CONCANAVALIN A/12-MER PEPTIDE COMPLEX

Summary for 1JYI
Entry DOI10.2210/pdb1jyi/pdb
Related1JOJ 1JUI 1JYC
DescriptorConcanavalin-Br, 12-mer peptide, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordslectin, sugar binding protein
Biological sourceCanavalia ensiformis (jack bean)
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Total number of polymer chains8
Total formula weight108331.38
Authors
Jain, D.,Kaur, K.J.,Sundaravadivel, B.,Salunke, D.M. (deposition date: 2001-09-12, release date: 2002-09-12, Last modification date: 2023-08-16)
Primary citationJain, D.,Kaur, K.J.,Sundaravadivel, B.,Salunke, D.M.
Structural and Functional Consequences of Peptide-carbohydrate Mimicry. Crystal Structure of a Carbohydrate-mimicking Peptide Bound to Concanavalin A.
J.Biol.Chem., 275:16098-16102, 2000
Cited by
PubMed Abstract: The functional consequences of peptide-carbohydrate mimicry were analyzed on the basis of the crystal structure of concanavalin A (ConA) in complex with a carbohydrate-mimicking peptide, DVFYPYPYASGS. The peptide binds to the non-crystallographically related monomers of two independent dimers of ConA in two different modes, in slightly different conformations, demonstrating structural adaptability in ConA-peptide recognition. In one mode, the peptide has maximum interactions with ConA, and in the other, it shows relatively fewer contacts within this site but significant contacts with the symmetry-related subunit. Neither of the peptide binding sites overlaps with the structurally characterized mannose and trimannose binding sites on ConA. Despite this, the functional mimicry between the peptide and carbohydrate ligands was evident. The peptide-inhibited ConA induced T cell proliferation in a dose-dependent manner. The effect of the designed analogs of the peptide on ConA-induced T cell proliferation and their recognition by the antibody response against alpha-d-mannopyranoside indicate a role for aromatic residues in functional mimicry. Although the functional mimicry was observed between the peptide and carbohydrate moieties, the crystal structure of the ConA-peptide complex revealed that the two peptide binding sites are independent of the methyl alpha-d-mannopyranoside binding site.
PubMed: 10821862
DOI: 10.1074/jbc.275.21.16098
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.75 Å)
Structure validation

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数据于2025-12-10公开中

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