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Updated: Jun 8, 2026

Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
Published on: March 16, 2020
Conformational changes in the g protein-coupled receptor rhodopsin revealed by histidine hydrogen-deuterium exchange
David T Lodowski1, Krzysztof Palczewski, Masaru Miyagi
1Department of Pharmacology, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106-4965, United States. dtl10@case.edu
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.
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