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Free backbone carbonyls mediate rhodopsin activation

Kimata, N and Pope, A and Sanchez-Reyes, OB and Eilers, M and Opefi, CA and Ziliox, M and Reeves, PJ and Smith, SO (2016) 'Free backbone carbonyls mediate rhodopsin activation.' Nature Structural and Molecular Biology, 23 (8). 738 - 743. ISSN 1545-9993

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© 2016 Nature America, Inc. All rights reserved. Conserved prolines in the transmembrane helices of G-protein-coupled receptors (GPCRs) are often considered to function as hinges that divide the helix into two segments capable of independent motion. Depending on their potential to hydrogen-bond, the free C=O groups associated with these prolines can facilitate conformational flexibility, conformational switching or stabilization of the receptor structure. To address the role of conserved prolines in family A GPCRs through solid-state NMR spectroscopy, we focus on bovine rhodopsin, a GPCR in the visual receptor subfamily. The free backbone C=O groups on helices H5 and H7 stabilize the inactive rhodopsin structure through hydrogen-bonds to residues on adjacent helices. In response to light-induced isomerization of the retinal chromophore, hydrogen-bonding interactions involving these C=O groups are released, thus facilitating repacking of H5 and H7 onto the transmembrane core of the receptor. These results provide insights into the multiple structural and functional roles of prolines in membrane proteins.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Philip Reeves
Date Deposited: 18 Aug 2016 09:20
Last Modified: 14 Oct 2019 17:22

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