Nature Communications (Jan 2022)
Crystal structure of the α1B-adrenergic receptor reveals molecular determinants of selective ligand recognition
- Mattia Deluigi,
- Lena Morstein,
- Matthias Schuster,
- Christoph Klenk,
- Lisa Merklinger,
- Riley R. Cridge,
- Lazarus A. de Zhang,
- Alexander Klipp,
- Santiago Vacca,
- Tasneem M. Vaid,
- Peer R. E. Mittl,
- Pascal Egloff,
- Stefanie A. Eberle,
- Oliver Zerbe,
- David K. Chalmers,
- Daniel J. Scott,
- Andreas Plückthun
Affiliations
- Mattia Deluigi
- Department of Biochemistry, University of Zurich
- Lena Morstein
- Department of Biochemistry, University of Zurich
- Matthias Schuster
- Department of Chemistry, University of Zurich
- Christoph Klenk
- Department of Biochemistry, University of Zurich
- Lisa Merklinger
- Department of Biochemistry, University of Zurich
- Riley R. Cridge
- The Florey Institute of Neuroscience and Mental Health, The University of Melbourne
- Lazarus A. de Zhang
- The Florey Institute of Neuroscience and Mental Health, The University of Melbourne
- Alexander Klipp
- Department of Biochemistry, University of Zurich
- Santiago Vacca
- Department of Biochemistry, University of Zurich
- Tasneem M. Vaid
- Department of Pharmaceutical Sciences, University of Illinois at Chicago
- Peer R. E. Mittl
- Department of Biochemistry, University of Zurich
- Pascal Egloff
- Department of Biochemistry, University of Zurich
- Stefanie A. Eberle
- Department of Biochemistry, University of Zurich
- Oliver Zerbe
- Department of Chemistry, University of Zurich
- David K. Chalmers
- Monash Institute of Pharmaceutical Sciences, Monash University
- Daniel J. Scott
- The Florey Institute of Neuroscience and Mental Health, The University of Melbourne
- Andreas Plückthun
- Department of Biochemistry, University of Zurich
- DOI
- https://doi.org/10.1038/s41467-021-27911-3
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 13
Abstract
This study reports the X-ray structure of the α1B-adrenergic G protein-coupled receptor bound to an inverse agonist, and unveils key determinants of subtype-selective ligand binding that may help the design of aminergic drugs with fewer side-effects.
