G-Protein coupled receptors: structure and function in drug discovery

Odoemelam, C.S., Percival, B., Wallis, H., Chang, M.-W., Ahmad, Z., Scholey, D. ORCID: 0000-0003-2450-5989, Burton, E. ORCID: 0000-0003-2784-6922, Williams, I.H., Kamerlin, C.L. and Wilson, P.B. ORCID: 0000-0003-0207-2246, 2020. G-Protein coupled receptors: structure and function in drug discovery. RSC Advances, 10 (60), pp. 36337-36348. ISSN 2046-2069

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Abstract

The G-protein coupled receptors (GPCRs) superfamily comprise similar proteins arranged into families or classes thus making it one of the largest in the mammalian genome. GPCRs take part in many vital physiological functions making them targets for numerous novel drugs. GPCRs share some distinctive features, such as the seven transmembrane domains, they also differ in the number of conserved residues in their transmembrane domain. Here we provide an introductory and accessible review detailing the computational advances in GPCR pharmacology and drug discovery. An overview is provided on family A-C GPCRs; their structural differences, GPCR signalling, allosteric binding and cooperativity. The dielectric constant (relative permittivity) of proteins is also discussed in the context of site-specific environmental effects.

Item Type: Journal article
Publication Title: RSC Advances
Creators: Odoemelam, C.S., Percival, B., Wallis, H., Chang, M.-W., Ahmad, Z., Scholey, D., Burton, E., Williams, I.H., Kamerlin, C.L. and Wilson, P.B.
Publisher: Royal Society of Chemistry (RSC)
Date: 1 October 2020
Volume: 10
Number: 60
ISSN: 2046-2069
Identifiers:
NumberType
10.1039/d0ra08003aDOI
1371372Other
Rights: This journal is © The Royal Society of Chemistry 2020. Open Access Article. Published on 01 October 2020. Downloaded on 11/16/2020 1:01:48 PM. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence.
Divisions: Schools > School of Animal, Rural and Environmental Sciences
Record created by: Linda Sullivan
Date Added: 02 Oct 2020 10:40
Last Modified: 31 May 2021 15:13
URI: http://irep.ntu.ac.uk/id/eprint/41103

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