Zdravkovic Igor, Zhao Chunfeng, Lev Bogdan, Cuervo Javier Eduardo, Noskov Sergei Yu
Institute for Biocomplexity and Informatics (IBI), University of Calgary, 2500 University Drive, Calgary, Canada, T2N 1N4.
Biochim Biophys Acta. 2012 Feb;1818(2):337-47. doi: 10.1016/j.bbamem.2011.10.031. Epub 2011 Nov 29.
The recent determination of high-resolution crystal structures of several transporters offers unprecedented insights into the structural mechanisms behind secondary transport. These proteins utilize the facilitated diffusion of the ions down their electrochemical gradients to transport the substrate against its concentration gradient. The structural studies revealed striking similarities in the structural organization of ion and solute binding sites and a well-conserved inverted-repeat topology between proteins from several gene families. In this paper we will overview recent atomistic simulations applied to study the mechanisms of selective binding of ion and substrate in LeuT, Glt, vSGLT and hSERT as well as its consequences for the transporter conformational dynamics. This article is part of a Special Issue entitled: Membrane protein structure and function.
最近对几种转运蛋白的高分辨率晶体结构的测定，为次级转运背后的结构机制提供了前所未有的见解。这些蛋白质利用离子顺着其电化学梯度的易化扩散来逆着底物的浓度梯度转运底物。结构研究揭示了离子和溶质结合位点的结构组织存在显著相似性，以及几个基因家族的蛋白质之间保守的反向重复拓扑结构。在本文中，我们将概述最近应用的原子模拟，以研究亮氨酸转运蛋白（LeuT）、谷氨酸转运体（Glt）、钠葡萄糖协同转运蛋白（vSGLT）和5-羟色胺转运体（hSERT）中离子和底物的选择性结合机制，以及其对转运蛋白构象动力学的影响。本文是名为“膜蛋白结构与功能”的特刊的一部分。
