1oaz
From Proteopedia
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'''IGE FV SPE7 COMPLEXED WITH A RECOMBINANT THIOREDOXIN''' | '''IGE FV SPE7 COMPLEXED WITH A RECOMBINANT THIOREDOXIN''' | ||
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[[Category: Roversi, P.]] | [[Category: Roversi, P.]] | ||
[[Category: Tawfik, D.]] | [[Category: Tawfik, D.]] | ||
| - | [[Category: | + | [[Category: Allergy]] |
| - | [[Category: | + | [[Category: Antibody]] |
| - | [[Category: | + | [[Category: Conformational diversity]] |
| - | [[Category: | + | [[Category: Ige]] |
| - | [[Category: | + | [[Category: Multispecficity,redox-active center,electron transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:36, 3 May 2008
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 Sat May 3 03:36:48 2008
