1jyc

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[[Image:1jyc.gif|left|200px]]
[[Image:1jyc.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1jyc", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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{{STRUCTURE_1jyc| PDB=1jyc | SCENE= }}
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|RELATEDENTRY=[[1joj|1JOJ]], [[1jui|1JUI]], [[1jyi|1JYI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyc OCA], [http://www.ebi.ac.uk/pdbsum/1jyc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jyc RCSB]</span>
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'''CONCANAVALIN A/15-mer PEPTIDE COMPLEX'''
'''CONCANAVALIN A/15-mer PEPTIDE COMPLEX'''
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[[Category: Kaur, K J.]]
[[Category: Kaur, K J.]]
[[Category: Salunke, D M.]]
[[Category: Salunke, D M.]]
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[[Category: lectin]]
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[[Category: Lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:04:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:44 2008''
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Revision as of 19:04, 2 May 2008

Template:STRUCTURE 1jyc

CONCANAVALIN A/15-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

1JYC is a Single protein structure of sequence from Canavalia ensiformis. 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 Page seeded by OCA on Fri May 2 22:04:28 2008

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