Crystal Structure of the OPG2 Fab AN ANTIRECEPTOR ANTIBODY THAT MIMICS AN RGD CELL ADHESION SITE
作者： Ramadurgam Kodandapani , B. Veerapandian , Thomas J. Kunicki , Kathryn R. Ely
关键词: Integrin 、 Cell adhesion 、 Fibronectin 、 Biophysics 、 Ligand (biochemistry) 、 Receptor 、 Antibody 、 Antireceptor antibody 、 Cell surface receptor 、 Biochemistry 、 Chemistry
摘要: 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 hemostasis is mediated by binding fibrinogen to gpIIb/IIIa integrin. The OPG2 antibody binds receptor acts a ligand mimic due presence an argininetyrosine-aspartic (RYD) CDR3 loop heavy chain. RYD side chains are ordered 2.0-A resolution crystal structure Fab fragment from this antireceptor antibody. Moreover, assumes two clearly defined conformations that may correspond orientations free state or bound This molecule will serve tool for understanding protein-integrin platelet other RGDmediated interactions.
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