Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 55, Issue 2, Pages 588-592Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201508648
Keywords
biophysics; flexible surface model; G-protein-coupled receptor; photoactivation; rhodopsin
Categories
Funding
- NSF [DMR-1410825, CBET-1160291]
- NIH
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Institute of General Medical Sciences [P41GM103393]
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [1623241] Funding Source: National Science Foundation
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [1623240] Funding Source: National Science Foundation
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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.
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