1jui: Difference between revisions
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[[Image:1jui.gif|left|200px]] | [[Image:1jui.gif|left|200px]] | ||
'''CONCANAVALIN A-CARBOHYDRATE MIMICKING 10-MER PEPTIDE COMPLEX''' | {{Structure | ||
|PDB= 1jui |SIZE=350|CAPTION= <scene name='initialview01'>1jui</scene>, resolution 2.75Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CONCANAVALIN A-CARBOHYDRATE MIMICKING 10-MER PEPTIDE COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JUI is a [ | 1JUI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUI OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11371463 11371463] | ||
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:41 2008'' | ||
Revision as of 13:08, 20 March 2008
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CONCANAVALIN A-CARBOHYDRATE MIMICKING 10-MER PEPTIDE COMPLEX
OverviewOverview
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 StructureAbout this Structure
1JUI is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
ReferenceReference
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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