1OPG
OPG2 FAB FRAGMENT
Summary for 1OPG
Entry DOI | 10.2210/pdb1opg/pdb |
Descriptor | OPG2 FAB (LIGHT CHAIN), OPG2 FAB (HEAVY CHAIN) (3 entities in total) |
Functional Keywords | cell adhesion molecule, immunoglobulin |
Biological source | Homo sapiens (human) More |
Cellular location | Isoform Secreted: Secreted: P01868 |
Total number of polymer chains | 2 |
Total formula weight | 48058.28 |
Authors | Kodandapani, R.,Veerapandian, B.,Ely, K.R. (deposition date: 1995-04-28, release date: 1995-07-31, Last modification date: 2024-06-05) |
Primary citation | Kodandapani, R.,Veerapandian, B.,Kunicki, T.J.,Ely, K.R. Crystal structure of the OPG2 Fab. An antireceptor antibody that mimics an RGD cell adhesion site. J.Biol.Chem., 270:2268-2273, 1995 Cited by PubMed Abstract: Cell surface receptors called integrins mediate diverse cell adhesion phenomena through recognition of the sequence arginine-glycine-aspartic acid (RGD) present in proteins such as fibronectin and fibrinogen. Platelet aggregation in hemostasis is mediated by the binding of fibrinogen to the gpIIb/IIIa integrin. The OPG2 antibody binds the gpIIb/IIIa receptor and acts as a ligand mimic due to the presence of an arginine-tyrosine-aspartic acid (RYD) sequence in the CDR3 loop of the heavy chain. The RYD loop and side chains are ordered in the 2.0-A resolution crystal structure of the Fab fragment from this antireceptor antibody. Moreover, the RYD loop assumes two clearly defined conformations that may correspond to the orientations of the loop in the free state or bound to integrin. This molecule will serve as a tool for understanding protein-integrin recognition in platelet aggregation and other RGD-mediated cell adhesion interactions. PubMed: 7836460DOI: 10.1074/jbc.270.5.2268 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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