1oaz
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1oaz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oaz, resolution 2.78Å" /> '''IGE FV SPE7 COMPLEX...)
Next diff →
Revision as of 07:32, 18 November 2007
|
IGE FV SPE7 COMPLEXED WITH A RECOMBINANT THIOREDOXIN
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
1OAZ is a Single protein structure of sequence from Escherichia coli and Rattus rattus. 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 Sun Nov 18 09:39:03 2007
