An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors - PubMed (original) (raw)
. 1997 Sep 12;272(1):144-64.
doi: 10.1006/jmbi.1997.1240.
Affiliations
- PMID: 9299344
- DOI: 10.1006/jmbi.1997.1240
An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
J M Baldwin et al. J Mol Biol. 1997.
Abstract
A model for the alpha-carbon positions in the seven transmembrane helices in the rhodopsin family of G-protein-coupled receptors is presented. The model incorporates structural information derived from the analysis of approximately 500 sequences in this family. The location, relative to the centre of the lipid bilayer, of each of the seven helical sequence segments and their probable lengths are deduced from sequence analysis, along with the orientation, relative to the centre of the helix bundle, of each helical segment around its axis. The packing of the helices in the model is guided by the density in a three-dimensional map of frog rhodopsin determined by electron cryo-microscopy. The model suggests which of the residues that are highly conserved in this family of receptors interact with each other. Helices III, V and VI are predicted to protrude more than the others from the central lipid core towards the aqueous phase on the intracellular side of the membrane. This feature could be a property of the receptor structure in some but not all of the conformations that it adopts, since recent studies suggest that relative movement occurs between these helices on photoactivation of rhodopsin. Results from other techniques, including the creation of metal-binding sites and disulphide bridges, site-directed spin-labelling studies, the substituted-cysteine accessibility method and other site-directed mutagenesis studies, are discussed in terms of the model.
Copyright 1997 Academic Press Limited.
Similar articles
- Structure of the integral membrane domain of the GLP1 receptor.
Frimurer TM, Bywater RP. Frimurer TM, et al. Proteins. 1999 Jun 1;35(4):375-86. Proteins. 1999. PMID: 10382665 - Arrangement of rhodopsin transmembrane alpha-helices.
Unger VM, Hargrave PA, Baldwin JM, Schertler GF. Unger VM, et al. Nature. 1997 Sep 11;389(6647):203-6. doi: 10.1038/38316. Nature. 1997. PMID: 9296501 - Structure of rhodopsin.
Schertler GF. Schertler GF. Novartis Found Symp. 1999;224:54-66; discussion 66-9,. Novartis Found Symp. 1999. PMID: 10614046 Review.
Cited by
- Structural aspects of rod opsin and their implication in genetic diseases.
Fanelli F, Felline A, Marigo V. Fanelli F, et al. Pflugers Arch. 2021 Sep;473(9):1339-1359. doi: 10.1007/s00424-021-02546-x. Epub 2021 Mar 16. Pflugers Arch. 2021. PMID: 33728518 Review. - Extracellular loops 2 and 3 of the calcitonin receptor selectively modify agonist binding and efficacy.
Dal Maso E, Zhu Y, Pham V, Reynolds CA, Deganutti G, Hick CA, Yang D, Christopoulos A, Hay DL, Wang MW, Sexton PM, Furness SGB, Wootten D. Dal Maso E, et al. Biochem Pharmacol. 2018 Apr;150:214-244. doi: 10.1016/j.bcp.2018.02.005. Epub 2018 Feb 16. Biochem Pharmacol. 2018. PMID: 29454620 Free PMC article. - Apelinergic System Structure and Function.
Shin K, Kenward C, Rainey JK. Shin K, et al. Compr Physiol. 2017 Dec 12;8(1):407-450. doi: 10.1002/cphy.c170028. Compr Physiol. 2017. PMID: 29357134 Free PMC article. Review. - Unconventional Roles of Opsins.
Leung NY, Montell C. Leung NY, et al. Annu Rev Cell Dev Biol. 2017 Oct 6;33:241-264. doi: 10.1146/annurev-cellbio-100616-060432. Epub 2017 Jun 9. Annu Rev Cell Dev Biol. 2017. PMID: 28598695 Free PMC article. Review. - Modeling of mammalian olfactory receptors and docking of odorants.
Launay G, Sanz G, Pajot-Augy E, Gibrat JF. Launay G, et al. Biophys Rev. 2012 Sep;4(3):255-269. doi: 10.1007/s12551-012-0080-0. Epub 2012 Sep 1. Biophys Rev. 2012. PMID: 28510073 Free PMC article. Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources