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Conformational restriction of G-proteins Coupled Receptors (GPCRs) upon complexation to G-proteins: A putative activation mode of GPCRs?

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
587
Issue
16
Identifiers
DOI: 10.1016/j.febslet.2013.06.052
Keywords
  • G-Protein Coupled Receptor
  • G-Protein Heterotrimer Complex
  • Normal Mode Analysis
  • Activation Mechanism
  • Unique Motion
Disciplines
  • Biology

Abstract

Abstract GPCRs undergo large conformational changes during their activation. Starting from existing X-ray structures, we used Normal Modes Analyses to study the collective motions of the agonist-bound β2-adrenergic receptor both in its isolated “uncoupled” and G-protein “coupled” conformations. We interestingly observed that the receptor was able to adopt only one major motion in the protein:protein complex. This motion corresponded to an anti-symmetric rotation of both its extra- and intra-cellular parts, with a key role of previously identified highly conserved proline residues. Because this motion was also retrieved when performing NMA on 7 other GPCRs which structures were available, it is strongly suspected to possess a significant biological role, possibly being the “activation mode” of a GPCR when coupled to G-proteins.

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