Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein

Tools
- Tools
+ Tools

García-Nafría, Javier, Lee, Yang, Bai, Xiaochen, Carpenter, Byron and Tate, Christopher G. (2018) Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein. eLife, 2018 (7). e35946. doi:10.7554/eLife.35946

[img]
Preview
PDF
WRAP-Cryo-EM-structure-of-the-adenosine-Carpenter-2018.pdf - Published Version - Requires a PDF viewer.
Available under License Creative Commons Attribution 4.0.

Download (6Mb) | Preview
Official URL: http://dx.doi.org/10.7554/eLife.35946

Request Changes to record.

Abstract

The adenosine A2A receptor (A2AR) is a prototypical G protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein GS. Here, we determine the structure by electron cryo-microscopy (cryo-EM) of A2AR at pH 7.5 bound to the small molecule agonist NECA and coupled to an engineered heterotrimeric G protein, which contains mini-GS, the βγ subunits and nanobody Nb35. Most regions of the complex have a resolution of ~3.8 Å or better. Comparison with the 3.4 Å resolution crystal structure shows that the receptor and mini-GS are virtually identical and that the density of the side chains and ligand are of comparable quality. However, the cryo-EM density map also indicates regions that are flexible in comparison to the crystal structures, which unexpectedly includes regions in the ligand binding pocket. In addition, an interaction between intracellular loop 1 of the receptor and the β subunit of the G protein was observed.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): G proteins, Ligand binding (Biochemistry)
Journal or Publication Title: eLife
Publisher: eLife Sciences Publications Ltd.
ISSN: 2050-084X
Official Date: 4 May 2018
Dates:
DateEvent
4 May 2018Published
2 May 2018Accepted
Date of first compliant deposit: 22 May 2018
Volume: 2018
Number: 7
Article Number: e35946
DOI: 10.7554/eLife.35946
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
339995H2020 European Research Councilhttp://dx.doi.org/10.13039/100010663
UNSPECIFIEDHeptares Therapeutics (Firm)UNSPECIFIED
UNSPECIFIEDPfizerhttp://dx.doi.org/10.13039/100004319
U105197215[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
Related URLs:
  • https://elifesciences.org/articles/35946
Open Access Version:
  • Publisher

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us