Conformational Changes in the G Protein-Coupled Receptor Rhodopsin Revealed by Histidine Hydrogen−Deuterium Exchange

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• 作者：David T. Lodowski ; Krzysztof Palczewski ; Masaru Miyagi
• 刊名：Biochemistry
• 出版年：2010
• 出版时间：November 9, 2010
• 年：2010
• 卷：49
• 期：44
• 页码：9425-9427
• 全文大小：710K
• 年卷期：v.49,no.44(November 9, 2010)
• ISSN：1520-4995

文摘

G protein-coupled receptors (GPCRs) are activated by ligand binding, allowing extracellular signals to be efficiently transmitted through the membrane to the G protein recognition site, 40 Å away. Utilizing His residues found spaced throughout the GPCR, rhodopsin, we used His hydrogen−deuterium exchange (His-HDX) to monitor long-time scale structural rearrangements previously inaccessible by other means. The half-lives of His-HDX indicate clear differences in the solvent accessibility of three His residues in rhodopsin/opsin and Zn²⁺-dependent changes in the pK_a for His¹⁹⁵. These results indicate the utility of His-HDX in examining structural rearrangements in native source and membrane proteins without requiring structural modification.