1oay
From Proteopedia
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Revision as of 14:43, 5 November 2007
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ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY
Overview
A single antibody was shown to adopt different binding-site conformations, and thereby bind unrelated antigens. Analysis by both x-ray, crystallography and pre-steady-state kinetics revealed an equilibrium, between different preexisting isomers, one of which possessed a, promiscuous, low-affinity binding site for aromatic ligands, including the, immunizing hapten. A subsequent induced-fit isomerization led to, high-affinity complexes with a deep and narrow binding site. A protein, antigen identified by repertoire selection made use of an unrelated, antibody isomer with a wide, shallow binding site. Conformational, diversity, whereby one sequence adopts multiple structures and multiple, functions, can increase the effective size of the antibody repertoire but, may also lead to autoimmunity and allergy.
About this Structure
1OAY is a Protein complex structure of sequences from Rattus rattus with FUR as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:12610298
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