1bm3 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Antibodies are important tools to explore receptor-ligand interactions. The anti-integrin antibody OPG2 binds in an RGD-related manner to the alphaIIb beta3 integrin as a molecular mimic of fibrinogen. The Fab fragment from OPG2 was cocrystallized with a peptide from the beta3 subunit of the integrin representing a site that binds RGD. The crystal structure of the complex was determined at 2.2-A resolution and compared with the unbound Fab. On binding the integrin peptide there were conformational changes in CDR3 of the heavy chain. Also, a significant shift across the intermolecular interface between the CH1-CL domains was observed so that the angle of rotation relating the two domains was reduced by 15 degrees. This unusual conformational adjustment represents the first example of ligand-induced conformational changes in the carboxyl domains of a Fab fragment.
Conformational change in an anti-integrin antibody: structure of OPG2 Fab bound to a beta 3 peptide.,Kodandapani R, Veerapandian L, Ni CZ, Chiou CK, Whittal RM, Kunicki TJ, Ely KR Biochem Biophys Res Commun. 1998 Oct 9;251(1):61-6. PMID:9790907[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Kodandapani R, Veerapandian L, Ni CZ, Chiou CK, Whittal RM, Kunicki TJ, Ely KR. Conformational change in an anti-integrin antibody: structure of OPG2 Fab bound to a beta 3 peptide. Biochem Biophys Res Commun. 1998 Oct 9;251(1):61-6. PMID:9790907 doi:10.1006/bbrc.1998.9380
