Fundación Pública Galega de Medicina Xenómica, Hospital Clínico Universitario de Santiago, E-15706, Santiago de Compostela, Spain.
Biochem Soc Trans. 2013 Feb 1;41(1):205-12. doi: 10.1042/BST20120287.
The recent advances in membrane protein crystallography have provided extremely valuable structural information of the superfamily of GPCRs (G-protein-coupled receptors). This has been particularly true for a few receptors whose structure was solved several times under different biochemical conditions. It follows that the mechanisms of receptor conformational equilibrium and related dynamic events can be explored by computational simulations. In the present article, we summarize our recent understanding of several dynamic features of GPCRs, accomplished through the use of MD (molecular dynamics) simulations. Our pipeline for the MD simulations of GPCRs, implemented in the web service http://gpcr.usc.es, is updated in the present paper and illustrated by recent applications. Special emphasis is put on the A2A adenosine receptor, one of the selected cases where crystal structures in several conformations and conditions exist, and on the dimerization process of the CXCR4 (CXC chemokine receptor 4).
膜蛋白晶体学的最新进展为 G 蛋白偶联受体（GPCR）超家族提供了极其有价值的结构信息。对于一些结构在不同生化条件下多次被解析的受体来说尤其如此。这意味着可以通过计算模拟来探索受体构象平衡和相关动态事件的机制。在本文中，我们通过使用 MD（分子动力学）模拟总结了我们对 GPCR 几个动态特征的最新理解。我们在网络服务 http://gpcr.usc.es 中实现的 GPCRs 的 MD 模拟管道在本文中进行了更新，并通过最近的应用进行了说明。特别强调了 A2A 腺苷受体，它是存在几种构象和条件的晶体结构的选定案例之一，以及 CXCR4（CXC 趋化因子受体 4）的二聚化过程。
