1jyc
From Proteopedia
(New page: 200px<br /><applet load="1jyc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jyc, resolution 2.75Å" /> '''CONCANAVALIN A/15-me...) |
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| - | [[Image:1jyc.gif|left|200px]]<br /><applet load="1jyc" size=" | + | [[Image:1jyc.gif|left|200px]]<br /><applet load="1jyc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jyc, resolution 2.75Å" /> | caption="1jyc, resolution 2.75Å" /> | ||
'''CONCANAVALIN A/15-mer PEPTIDE COMPLEX'''<br /> | '''CONCANAVALIN A/15-mer PEPTIDE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of concanavalin A (ConA) in complex with two | + | 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== | ==About this Structure== | ||
| - | 1JYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1JYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jain, D.]] | [[Category: Jain, D.]] | ||
| - | [[Category: Kaur, K | + | [[Category: Kaur, K J.]] |
| - | [[Category: Salunke, D | + | [[Category: Salunke, D M.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:06 2008'' |
Revision as of 11:28, 21 February 2008
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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 with and 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
Page seeded by OCA on Thu Feb 21 13:28:06 2008
Categories: Canavalia ensiformis | Single protein | Jain, D. | Kaur, K J. | Salunke, D M. | CA | MN | Lectin
