1oay
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(New page: 200px<br /> <applet load="1oay" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oay, resolution 2.66Å" /> '''ANTIBODY MULTISPECI...)
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Revision as of 17:49, 29 October 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 ... [(full description)]
About this Structure
1OAY is a [Protein complex] structure of sequences from [Rattus rattus] with FUR as [ligand]. 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
Page seeded by OCA on Mon Oct 29 19:54:09 2007
