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The role of NMR spectroscopy in mapping the conformational landscape of GPCRs.

Accepted version
Peer-reviewed

Type

Article

Change log

Authors

Bostock, Mark J 
Solt, Andras S 
Nietlispach, Daniel  ORCID logo  https://orcid.org/0000-0003-4364-9291

Abstract

Over recent years, nuclear magnetic resonance (NMR) spectroscopy has developed into a powerful mechanistic tool for the investigation of G protein-coupled receptors (GPCRs). NMR provides insights which underpin the dynamic nature of these important receptors and reveals experimental evidence for a complex conformational energy landscape that is explored during receptor activation resulting in signalling. NMR studies have highlighted both the dynamic properties of different receptor states as well as the exchange pathways and intermediates formed during activation, extending the static view of GPCRs obtained from other techniques. NMR studies can be undertaken in realistic membrane-like phospholipid environments and an ever-increasing choice of labelling strategies provides comprehensive, receptor-wide information. Combined with other structural methods, NMR is contributing to our understanding of allosteric signal propagation and the interaction of GPCRs with intracellular binding partners (IBP), crucial to explaining cellular signalling.

Description

Keywords

Animals, Humans, Ligands, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Receptors, G-Protein-Coupled

Journal Title

Curr Opin Struct Biol

Conference Name

Journal ISSN

0959-440X
1879-033X

Volume Title

57

Publisher

Elsevier BV
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/K01983X/1)
MRC (MR/L014254/1)
Biotechnology and Biological Sciences Research Council (BB/G011915/1)
Biotechnology and Biological Sciences Research Council (BB/S015892/1)
BBSRC BB/K01983 X/1