1jui

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Revision as of 16:28, 20 November 2007

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spinqualitylabelsall models 1jui, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CONCANAVALIN A-CARBOHYDRATE MIMICKING 10-MER PEPTIDE COMPLEX

Overview

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.

About this Structure

1JUI is a Single protein structure of sequence from Canavalia ensiformis with MN and CA as ligands. Full crystallographic information is available from OCA.

Reference

Plasticity in protein-peptide recognition: crystal structures of two different peptides bound to concanavalin A., Jain D, Kaur KJ, Salunke DM, Biophys J. 2001 Jun;80(6):2912-21. PMID:11371463

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