1joj: Difference between revisions

Revision as of 20:33, 1 July 2008

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File:1joj.png

Template:STRUCTURE 1joj

CONCANAVALIN A-HEXAPEPTIDE COMPLEXCONCANAVALIN A-HEXAPEPTIDE COMPLEX

Template:ABSTRACT PUBMED 11580281

About this StructureAbout this Structure

1JOJ is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

ReferenceReference

Enhanced binding of a rationally designed peptide ligand of concanavalin a arises from improved geometrical complementarity., Jain D, Kaur KJ, Salunke DM, Biochemistry. 2001 Oct 9;40(40):12059-66. PMID:11580281

Page seeded by OCA on Tue Jul 1 20:33:34 2008

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OCA

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-[[Image:1joj.gif|left|200px]]
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 {{STRUCTURE_1joj|  PDB=1joj  |  SCENE=  }}
-'''CONCANAVALIN A-HEXAPEPTIDE COMPLEX'''
+===CONCANAVALIN A-HEXAPEPTIDE COMPLEX===
-==Overview==
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-The structural basis of affinity enhancement was addressed by analyzing the interactions between concanavalin A and the carbohydrate-mimicking peptide ligands. Based on the crystal structures of concanavalin A in complex with these peptides [Jain, D., Kaur, K. J., Sundaravadivel, B., and Salunke, D. M. (2000) J. Biol. Chem. 275, 16098-16102; Jain, D., Kaur, K. J., and Salunke, D. M. (2001) Biophys. J. 80, 2912-2921], a high-affinity analogue was designed. This analogue (acetyl-MYWYPY-amide) binds to the lectin with 32-fold enhanced affinity compared to the corresponding precursor peptides. The crystal structure of concanavalin A bound to the designed peptide has been determined. A peptide molecule binds to each of the crystallographically independent monomers of the tetrameric lectin. The four bound peptide molecules exhibit two major conformations both of which are extended. Unlike in the case of other concanavalin A binding peptides, the structural variations within different conformers of this analogue are marginal. It is apparent that the deletion of the structurally variable region of the larger peptides has led to an improved complementarity and increased buried surface area in the case of the designed peptide. The crystal structure also showed the formation of two backbone hydrogen bonds between the ligand and the ligate which were not present in the complexes of the precursor peptides. The observed structural features adequately explain the enhanced binding of the designed analogue.
+The line below this paragraph, {{ABSTRACT_PUBMED_11580281}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11580281 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11580281}}
 ==About this Structure==
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 [[Category: Salunke, D M.]]
 [[Category: Lectin]]
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