A structural basis for how ligand binding site changes can allosterically regulate GPCR signaling and engender functional selectivity-Reference-Cited by-同舟云学术

A structural basis for how ligand binding site changes can allosterically regulate GPCR signaling and engender functional selectivity

Published:2020-02-04 Issue:617 Volume:13 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Sanchez-Soto Marta¹^ORCID,Verma Ravi Kumar²,Willette Blair K. A.¹^ORCID,Gonye Elizabeth C.¹^ORCID,Moore Annah M.¹,Moritz Amy E.¹,Boateng Comfort A.³,Yano Hideaki²^ORCID,Free R. Benjamin¹^ORCID,Shi Lei²^ORCID,Sibley David R.¹^ORCID

Affiliation:

1. Molecular Neuropharmacology Section, NINDS, NIH, 35 Convent Drive, Room 3A201, Bethesda, MD 20892, USA.

2. Computational Chemistry and Molecular Biophysics Unit, NIDA, NIH, TRIAD Technology Center, 333 Cassell Drive, Room 1121, Baltimore, MD 21224, USA.

3. Basic Pharmaceutical Sciences, High Point University, One University Parkway, High Point, NC 27268, USA.

Abstract

A conserved amino acid residue in the ligand binding site of class A GPCRs regulates receptor interactions with β-arrestin.

Funder

National Institute on Drug Abuse

National Institute of Neurological Disorders and Stroke

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference76 articles.

1. The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

2. β-arrestin-mediated receptor trafficking and signal transduction

3. Structural Basis of Arrestin-Dependent Signal Transduction

4. The Diverse Roles of Arrestin Scaffolds in G Protein–Coupled Receptor Signaling

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