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The DOI matches its Crossref record; 157 of the 157 references it cites were found in a registry or an index.

GPCR Dynamics: Structures in Motion

Open access
Latorraca, Naomi R., Venkatakrishnan, A. J., Dror, Ron O.·2017·Chemical Reviews

Abstract

The function of G protein-coupled receptors (GPCRs)-which represent the largest class of both human membrane proteins and drug targets-depends critically on their ability to change shape, transitioning among distinct conformations. Determining the structural dynamics of GPCRs is thus essential both for understanding the physiology of these receptors and for the rational design of GPCR-targeted drugs. Here we review what is currently known about the flexibility and dynamics of GPCRs, as determined through crystallography, spectroscopy, and computer simulations. We first provide an overview of the types of motion exhibited by a GPCR and then discuss GPCR dynamics in the context of ligand binding, activation, allosteric modulation, and biased signaling. Finally, we discuss the implications of GPCR conformational plasticity for drug design.

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Crossref · 10.1021/acs.chemrev.6b00177

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Metadata

Authors
Latorraca, N. R., Venkatakrishnan, A. J., & Dror, R. O.
Venue
Chemical Reviews
Published
2016-09-13
Volume
117
Issue
1
Pages
139-155
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W2520075163
Cited by
835
References
157
FWCI
4.15
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: GPCR Dynamics: Structures in Motion. https://app.cochat.ai/papers/10.1021/acs.chemrev.6b00177
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Latorraca, N. R., Venkatakrishnan, A. J., & Dror, R. O. (2017). GPCR Dynamics: Structures in Motion. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.6b00177

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.