Department of Physiology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
J Physiol. 2010 Jan 1;588(Pt 1):59-66. doi: 10.1113/jphysiol.2009.179705.
Functional studies of the ligand gated ion channel family (nicotinic acetylcholine, serotonin Type 3, glycine and GABA receptors) along with the crystal structure of the acetylcholine binding protein (AChBP) and molecular dynamics simulations of the nAChR structure have resulted in a structural model in which the agonist-binding pocket comprises six loops (A-F) contributed by adjacent subunits. It is presumed that the binding of agonist results in a local structural rearrangement that is then transduced to the gate, causing the pore to open. Efforts are underway to better define the specific roles of the six binding loops. Several studies have suggested Loop F may play a direct role in linking the structural rearrangement within the binding pocket to the gate, although other investigations have indicated Loop F may be crucial for locking the agonist molecule into the binding site. This review will focus on the controversy surrounding the role of Loop F during GABA receptor activation.
配体门控离子通道家族（烟碱型乙酰胆碱、5-羟色胺 3 型、甘氨酸和 GABA 受体）的功能研究，以及乙酰胆碱结合蛋白（AChBP）的晶体结构和烟碱型乙酰胆碱受体结构的分子动力学模拟，产生了一个结构模型，其中激动剂结合口袋由相邻亚基贡献的六个环（A-F）组成。据推测，激动剂的结合导致局部结构重排，然后传递到门，导致孔打开。目前正在努力更好地定义六个结合环的具体作用。几项研究表明，环 F 可能在将结合口袋内的结构重排与门连接起来方面发挥直接作用，尽管其他研究表明环 F 对于将激动剂分子锁定在结合位点可能至关重要。这篇综述将集中讨论围绕环 F 在 GABA 受体激活过程中的作用的争议。
