CRYSTALLIZATION OF THE OP-G2 FAB FRAGMENT - A FIBRINOGEN MIMIC WITH SPECIFICITY FOR THE PLATELET GLYCOPROTEIN-IIB IIIA/

Authors
CELIKEL R WILLIAMSON MM NI CZ ELY KR KUNICKI TJ
Citation
R. Celikel et al., CRYSTALLIZATION OF THE OP-G2 FAB FRAGMENT - A FIBRINOGEN MIMIC WITH SPECIFICITY FOR THE PLATELET GLYCOPROTEIN-IIB IIIA/, Acta crystallographica. Section D, Biological crystallography, 49, 1993, pp. 421-422
Citations number
15
Categorie Soggetti
Crystallography,Biology,"Pharmacology & Pharmacy
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
49
Year of publication
1993
Part
4
Pages
421 - 422
Database
ISI
SICI code
0907-4449(1993)49:<421:COTOFF>2.0.ZU;2-6
Abstract
The OP-G2 monoclonal antibody binds to the platelet integrin, gpIIb/II Ia, in a mode that mimics fibrinogen binding. The specificity of this antibody is mediated by the third complementarity-determining region ( CDR3) loop of the immunoglobulin heavy chain which contains a sequence (RYD) related to the RGD recognition sequence of fibrinogen. The OP-G 2 Fab fragment has been crystallized by vapor diffusion from solutions containing polyethylene glycol and imidazole malate (pH 5.6). The cry stals belong to space group P2(1)2(1)2 with a = 93.1, b = 83.8 and c = 53.7 angstrom. One Fab molecule is present in the asymmetric unit. A complete data set to 2.0 angstrom resolution has been collected.