1BM3

IMMUNOGLOBULIN OPG2 FAB-PEPTIDE COMPLEX

Summary for 1BM3

• Entry DOI: 10.2210/pdb1bm3/pdb
• Descriptor: IMMUNOGLOBULIN OPG2 FAB, CONSTANT DOMAIN, IMMUNOGLOBULIN OPG2 FAB, VARIABLE DOMAIN (3 entities in total)
• Functional Keywords: immunoglobulin, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 48058.28

Authors

Kodandapani, R.,Veerapandian, L.,Ni, C.Z.,Chiou, C.-K.,Whital, R.,Kunicki, T.J.,Ely, K.R. (deposition date: 1999-04-15, release date: 1999-04-20, Last modification date: 2024-10-30)

Primary citation

Kodandapani, R.,Veerapandian, L.,Ni, C.Z.,Chiou, C.K.,Whittal, R.M.,Kunicki, T.J.,Ely, K.R.
Conformational change in an anti-integrin antibody: structure of OPG2 Fab bound to a beta 3 peptide.
Biochem.Biophys.Res.Commun., 251:61-66, 1998

PubMed Abstract: 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.

PubMed: 9790907
DOI: 10.1006/bbrc.1998.9380

Experimental method

X-RAY DIFFRACTION (2 Å)