Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, UK.
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, UK.
Curr Opin Struct Biol. 2019 Aug;57:145-156. doi: 10.1016/j.sbi.2019.03.030. Epub 2019 May 7.
Over recent years, nuclear magnetic resonance (NMR) spectroscopy has developed into a powerful mechanistic tool for the investigation of G protein-coupled receptors (GPCRs). NMR provides insights which underpin the dynamic nature of these important receptors and reveals experimental evidence for a complex conformational energy landscape that is explored during receptor activation resulting in signalling. NMR studies have highlighted both the dynamic properties of different receptor states as well as the exchange pathways and intermediates formed during activation, extending the static view of GPCRs obtained from other techniques. NMR studies can be undertaken in realistic membrane-like phospholipid environments and an ever-increasing choice of labelling strategies provides comprehensive, receptor-wide information. Combined with other structural methods, NMR is contributing to our understanding of allosteric signal propagation and the interaction of GPCRs with intracellular binding partners (IBP), crucial to explaining cellular signalling.
近年来，核磁共振（NMR）光谱已发展成为研究 G 蛋白偶联受体（GPCR）的强大机制工具。NMR 提供了深入了解这些重要受体动态特性的见解，并为受体激活过程中探索的复杂构象能量景观提供了实验证据，从而导致信号转导。NMR 研究强调了不同受体状态的动态特性，以及在激活过程中形成的交换途径和中间体，从而扩展了从其他技术获得的 GPCR 的静态观点。NMR 研究可以在逼真的类膜磷脂环境中进行，并且不断增加的标记策略选择提供了全面的、受体广泛的信息。与其他结构方法结合使用，NMR 有助于我们理解变构信号转导和 GPCR 与细胞内结合伙伴（IBP）的相互作用，这对于解释细胞信号转导至关重要。
