科研之友
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摘要
During the past decade, advanced techniques in structural biology have provided atomic level information on the platelet integrin IIb3 activation mechanism that results in it adopting a high-affinity ligand-binding conformation(s). This review focuses on advances in imaging intact IIb3 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 IIb3 antagonists being developed based on an advanced knowledge of the receptor's structure.
- 出版日期2015-6
