Porter Neuroscience Research Center, NINDS, NIH, 35A Convent Drive Room 3D 904, Bethesda, MD, 20892, USA.
Neuropharmacology. 2021 Jun 1;190:108511. doi: 10.1016/j.neuropharm.2021.108511. Epub 2021 Mar 30.
This review summarizes structural studies on kainate receptors that explain unique functional properties of this receptor family. A large number of structures have been solved for ligand binding domain dimer assemblies, giving insight into the subtype selective pharmacology of agonists, antagonists, and allosteric modulators. Structures and biochemical studies on the amino terminal domain reveal mechanisms that play a key role in assembly of heteromeric receptors. Surprisingly, structures of full length homomeric GluK2, GluK3 and heteromeric GluK2/GluK5, receptors reveal a novel structure for the desensitized state that is strikingly different from that for AMPA receptors.
这篇综述总结了关于激动型氨基酸受体（kainate receptor）的结构研究，这些研究解释了该受体家族独特的功能特性。已经有大量配体结合域二聚体组装的结构被解析，为激动剂、拮抗剂和别构调节剂的亚型选择性药理学提供了深入了解。关于氨基末端结构域的结构和生化研究揭示了在异源受体组装中起关键作用的机制。令人惊讶的是，全长同源 GluK2、GluK3 和异源 GluK2/GluK5 受体的结构揭示了一种新型的脱敏状态结构，与 AMPA 受体的结构明显不同。
