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- W2183023998 abstract "G-protein-coupled receptors (GPCRs) are the largest family of membrane-bound receptors and constitute about 50% of all known drug targets. They offer great potential for membrane protein nanotechnologies. We report here a charge-interaction-directed reconstitution mechanism that induces spontaneous insertion of bovine rhodopsin, the eukaryotic GPCR, into both lipid- and polymer-based artificial membranes. We reveal a new allosteric mode of rhodopsin activation incurred by the non-biological membranes: the cationic membrane drives a transition from the inactive MI to the activated MII state in the absence of high [H(+)] or negative spontaneous curvature. We attribute this activation to the attractive charge interaction between the membrane surface and the deprotonated Glu134 residue of the rhodopsin-conserved ERY sequence motif that helps break the cytoplasmic ionic lock. This study unveils a novel design concept of non-biological membranes to reconstitute and harness GPCR functions in synthetic systems." @default.
- W2183023998 created "2016-06-24" @default.
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- W2183023998 date "2015-12-03" @default.
- W2183023998 modified "2023-10-03" @default.
- W2183023998 title "A Usual G-Protein-Coupled Receptor in Unusual Membranes" @default.
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- W2183023998 doi "https://doi.org/10.1002/anie.201508648" @default.
- W2183023998 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5233722" @default.
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