Kimata, Naoki and Pope, Andreyah and Sanchez-Reyes, Omar B and Eilers, Markus and Opefi, Chikwado A and Ziliox, Martine and Reeves, Philip J and Smith, Steven O (2016) Free backbone carbonyls mediate rhodopsin activation. Nature Structural and Molecular Biology, 23 (8). pp. 738-743. DOI https://doi.org/10.1038/nsmb.3257
Kimata, Naoki and Pope, Andreyah and Sanchez-Reyes, Omar B and Eilers, Markus and Opefi, Chikwado A and Ziliox, Martine and Reeves, Philip J and Smith, Steven O (2016) Free backbone carbonyls mediate rhodopsin activation. Nature Structural and Molecular Biology, 23 (8). pp. 738-743. DOI https://doi.org/10.1038/nsmb.3257
Kimata, Naoki and Pope, Andreyah and Sanchez-Reyes, Omar B and Eilers, Markus and Opefi, Chikwado A and Ziliox, Martine and Reeves, Philip J and Smith, Steven O (2016) Free backbone carbonyls mediate rhodopsin activation. Nature Structural and Molecular Biology, 23 (8). pp. 738-743. DOI https://doi.org/10.1038/nsmb.3257
Abstract
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 |
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Uncontrolled Keywords: | Animals; Cattle; Humans; Ketones; Transducin; Rhodopsin; Allosteric Regulation; Protein Binding; Hydrogen Bonding; Models, Molecular; Light Signal Transduction; HEK293 Cells; Protein Conformation, alpha-Helical |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 18 Aug 2016 09:20 |
Last Modified: | 30 Oct 2024 20:12 |
URI: | http://repository.essex.ac.uk/id/eprint/17359 |
Available files
Filename: kimata_nsmb revised_v18.pdf