Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Structure-function of the G protein-coupled receptor superfamily

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Katritch, Vsevolod
  • Cherezov, Vadim
  • Stevens, Raymond

publication date

  • 2013

journal

  • Annual Review of Pharmacology and Toxicology  Journal

abstract

  • During the past few years, crystallography of G protein-coupled receptors (GPCRs) has experienced exponential growth, resulting in the determination of the structures of 16 distinct receptors-9 of them in 2012 alone. Including closely related subtype homology models, this coverage amounts to approximately 12% of the human GPCR superfamily. The adrenergic, rhodopsin, and adenosine receptor systems are also described by agonist-bound active-state structures, including a structure of the receptor-G protein complex for the β(2)-adrenergic receptor. Biochemical and biophysical techniques, such as nuclear magnetic resonance and hydrogen-deuterium exchange coupled with mass spectrometry, are providing complementary insights into ligand-dependent dynamic equilibrium between different functional states. Additional details revealed by high-resolution structures illustrate the receptors as allosteric machines that are controlled not only by ligands but also by ions, lipids, cholesterol, and water. This wealth of data is helping redefine our knowledge of how GPCRs recognize such a diverse array of ligands and how they transmit signals 30 angstroms across the cell membrane; it also is shedding light on a structural basis of GPCR allosteric modulation and biased signaling.

subject areas

  • Allosteric Regulation
  • Cell Membrane
  • Humans
  • Ligands
  • Models, Molecular
  • Protein Conformation
  • Receptors, G-Protein-Coupled
  • Structure-Activity Relationship
scroll to property group menus

Research

keywords

  • GPCR structure
  • activation
  • allosteric modulation
  • biased signaling
  • dimerization
  • diversity
  • ligand recognition
scroll to property group menus

Identity

PubMed Central ID

  • PMC3540149

International Standard Serial Number (ISSN)

  • 1545-4304 (Electronic) 0362-1642 (Linking)

Digital Object Identifier (DOI)

  • 10.1146/annurev-pharmtox-032112-135923

PubMed ID

  • 23140243
scroll to property group menus

Additional Document Info

start page

  • 531

end page

  • 556

volume

  • 53

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support