1oay: Difference between revisions

Revision as of 07:17, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oay.png

Template:STRUCTURE 1oay

ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITYANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY

Template:ABSTRACT PUBMED 12610298

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:12610298

Page seeded by OCA on Mon Jul 28 07:17:47 2008

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OCA

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-'''ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY'''
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-==Overview==
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-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.
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 ==About this Structure==
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 [[Category: Ige]]
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-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:36:48 2008''
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