Coller B S
Rockefeller University, New York, NY, USA.
J Thromb Haemost. 2015 Jun;13 Suppl 1(Suppl 1):S17-25. doi: 10.1111/jth.12915.
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.
在过去十年中，结构生物学的先进技术提供了关于血小板整合素αIIbβ3激活机制的原子水平信息，该机制导致其采用高亲和力配体结合构象。本综述重点关注在无去污剂的脂质双层中对完整αIIbβ3进行成像的进展，以及受体激活和配体结合时配体结合口袋变化的新结构见解。最后描述了基于对受体结构的深入了解而正在开发的新型治疗性αIIbβ3拮抗剂。
