title: αIIbβ3: structure and function.
abstract: During the past decade, advanced techniques in structural biology have provided atomic level information on the platelet integrin αIIbβ3 activation mechanism that results in it adopting a high-affinity ligand-binding conformation(s). This review focuses on advances in imaging intact αIIbβ3 in a lipid bilayer in the absence of detergent and new structural insights into the changes in the ligand-binding pocket with receptor activation and ligand binding. It concludes with descriptions of novel therapeutic αIIbβ3 antagonists being developed based on an advanced knowledge of the receptor's structure.
authors.affiliation: Rockefeller University, New York, NY, USA.
authors.forename: B S
authors.initials: BS
authors.lastname: Coller
mesh_terms: D000818:Animals; D001665:Binding Sites; D001792:Blood Platelets / Q000187:drug effects / Q000378:metabolism*; D015195:Drug Design; D006487:Hemostasis / Q000187:drug effects; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D010975:Platelet Aggregation Inhibitors / Q000627:therapeutic use; D019039:Platelet Glycoprotein GPIIb-IIIa Complex / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D015398:Signal Transduction; D013329:Structure-Activity Relationship
chemical_list: D008024:Ligands; D010975:Platelet Aggregation Inhibitors; D019039:Platelet Glycoprotein GPIIb-IIIa Complex
keywords: electron microscopy; integrin alphaIIbbeta3; platelet; thrombosis; x‐ray crystallography