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

ABSTRACT: 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.

SUBMITTER: Lodowski DT

PROVIDER: S-EPMC3075965 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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

Lodowski David T DT Palczewski Krzysztof K Miyagi Masaru M

Biochemistry 20101015 44

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 H ...[more]

PMID: 20939497

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