1oau
From Proteopedia
|
FV STRUCTURE OF THE IGE SPE-7 IN COMPLEX WITH DNP-SER (IMMUNISING HAPTEN)
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
1OAU is a [Single protein] structure of sequence from [Rattus rattus] with SER and IMD as [ligands]. 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
Page seeded by OCA on Tue Oct 30 15:48:28 2007
Categories: Rattus rattus | Single protein | James, L.C. | Roversi, P. | Tawfik, D. | IMD | SER | Allergy | Antibody | Conformational diversity | Ige | Multispecificity
