Conformational changes in the g protein-coupled receptor rhodopsin revealed by histidine hydrogen-deuterium exchange.

Conformational changes in the g protein-coupled receptor rhodopsin revealed by histidine hydrogen-deuterium exchange.
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DOI:
10.1021/bi101502v
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发表时间:
2010-11-09
期刊:
影响因子:
2.9
通讯作者:
Miyagi, Masaru
Miyagi, Masaru
中科院分区:
生物学3区
文献类型:
--
作者:
Lodowski, David T.;Palczewski, Krzysztof;Miyagi, Masaru

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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 pKa for His195. These results indicate the utility of His-HDX in examining structural rearrangements in native source and membrane proteins without requiring structural modification.
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