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Conformational dynamics of a G protein-coupled receptor helix 8 in lipid membranes

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Dijkman, Patricia M., Muñoz-García, Juan C., Steven R., Lavington, Suemy Kumagai, Patricia , dos Reis, Rosana I., Yin, Daniel , Stansfeld, Phillip J., Costa-Filho, Antonio José and Watt , Anthony (2020) Conformational dynamics of a G protein-coupled receptor helix 8 in lipid membranes. Science Advances, 6 (33). eaav8207. doi:10.1126/sciadv.aav8207

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Official URL: https://doi.org/10.1126/sciadv.aav8207

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Abstract

G protein–coupled receptors (GPCRs) are the largest and pharmaceutically most important class of membrane proteins encoded in the human genome, characterized by a seven-transmembrane helix architecture and a C-terminal amphipathic helix 8 (H8). In a minority of GPCR structures solved to date, H8 either is absent or adopts an unusual conformation. The controversial existence of H8 of the class A GPCR neurotensin receptor 1 (NTS1) has been examined here for the nonthermostabilized receptor in a functionally supporting membrane environment using electron paramagnetic resonance, molecular dynamics simulations, and circular dichroism. Lipid-protein interactions with phosphatidylserine and phosphatidylethanolamine lipids, in particular, stabilize the residues 374 to 390 of NTS1 into forming a helix. Furthermore, introduction of a helix-breaking proline residue in H8 elicited an increase in ß-arrestin–NTS1 interactions observed in pull-down assays, suggesting that the structure and/or dynamics of H8 might play an important role in GPCR signaling.

Item Type: Journal Article
Subjects: Q Science > QH Natural history > QH426 Genetics
R Medicine > RM Therapeutics. Pharmacology
Divisions: Faculty of Science > Chemistry
Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): G proteins -- Receptors, Drug development -- Research, Human genome, Human gene mapping
Journal or Publication Title: Science Advances
Publisher: American Association for the Advancement of Science
ISSN: 2375-2548
Official Date: 2020
Dates:
DateEvent
2020Published
14 August 2020Available
2 July 2020Accepted
Volume: 6
Number: 33
Article Number: eaav8207
DOI: 10.1126/sciadv.aav8207
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Copyright Holders: Copyright © 2020 The Authors
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
EP/R029407/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
G0900076[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
MR/S009213/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
BB/P01948X/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/R002517/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/S003339/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
208361/Z/17/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
2010/17662-8Fundação de Amparo à Pesquisa do Estado de São Paulohttp://viaf.org/viaf/147398725
2011/21767-2Fundação de Amparo à Pesquisa do Estado de São Paulohttp://viaf.org/viaf/147398725
2012/20358-4Fundação de Amparo à Pesquisa do Estado de São Paulohttp://viaf.org/viaf/147398725
UNSPECIFIEDConselho Nacional de Desenvolvimento Científico e Tecnológicohttp://dx.doi.org/10.13039/501100003593
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