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1JYC

CONCANAVALIN A/15-mer PEPTIDE COMPLEX

Summary for 1JYC
Entry DOI10.2210/pdb1jyc/pdb
Related1JOJ 1JUI 1JYI
DescriptorConcanavalin-Br, 15-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 weight109701.05
Authors
Jain, D.,Kaur, K.J.,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.,Salunke, D.M.
Plasticity in Protein-Peptide Recognition: Crystal Structures of Two Different Peptides Bound to Concanavalin A
Biophys.J., 80:2912-2921, 2001
Cited by
PubMed Abstract: The structures of concanavalin A (ConA) in complex with two carbohydrate-mimicking peptides, 10-mer (MYWYPYASGS) and 15-mer (RVWYPYGSYLTASGS) have been determined at 2.75 A resolution. In both crystal structures four independent peptide molecules bind to each of the crystallographically independent subunits of ConA tetramer. The peptides exhibit small but significant variability in conformations and interactions while binding to ConA. The crystal structure of another similar peptide, 12-mer (DVFYPYPYASGS), in complex with ConA has been determined (Jain, D., K. J. Kaur, B. Sundaravadivel, and D. M. Salunke. 2000. Structural and functional consequences of peptide-carbohydrate mimicry. J. Biol. Chem. 275:16098-16102). Comparison of the three complexes shows that the peptides bind to ConA at a common binding site, using different contacting residues and interactions depending on their sequence and the local environment at the binding site. The binding is also optimized by corresponding plasticity of the peptide binding site on ConA. The diversity in conformation and interactions observed here are in agreement with the structural leeway concerning plasticity of specific molecular recognition in biological processes. The adaptability of peptide-ConA interactions may also be correlated with the carbohydrate-mimicking property of these peptides.
PubMed: 11371463
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.75 Å)
Structure validation

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