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A Usual G-Protein-Coupled Receptor in Unusual Membranes.


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.

SUBMITTER: Chawla U 

PROVIDER: S-EPMC5233722 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature

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A Usual G-Protein-Coupled Receptor in Unusual Membranes.

Chawla Udeep U   Jiang Yunjiang Y   Zheng Wan W   Kuang Liangju L   Perera Suchithranga M D C SM   Pitman Michael C MC   Brown Michael F MF   Liang Hongjun H  

Angewandte Chemie (International ed. in English) 20151203 2


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 memb  ...[more]

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