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Published on: June 7, 2016

An angiotensin II type 1 receptor activation switch patch revealed through evolutionary trace analysis.

Marie Mi Bonde1, Rong Yao, Jian-Nong Ma

  • 1Laboratory for Molecular Cardiology, The Danish National Research Foundation Centre for Cardiac Arrhythmia, The Heart Centre, Copenhagen University Hospital, Rigshospitalet, Juliane Mariesvej 20, section 9312, DK-2100 Copenhagen, Denmark.

Biochemical Pharmacology
|March 16, 2010
PubMed
Summary

Evolutionary Trace analysis identified a conserved residue patch in seven transmembrane (7TM) receptors that acts as an activation switch. Mutations in this switch region of the Angiotensin II type 1a receptor altered its activation, supporting its role in 7TM receptor function.

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Area of Science:

  • Biochemistry
  • Computational Biology
  • Pharmacology

Background:

  • Seven transmembrane (7TM) receptors, also known as G protein-coupled receptors (GPCRs), are crucial cell surface proteins with a conserved seven alpha-helical transmembrane structure.
  • The precise mechanism of 7TM receptor activation, involving transmembrane helix movements, remains incompletely understood.

Purpose of the Study:

  • To investigate the role of a computationally predicted "activation switch" patch in 7TM receptor function.
  • To validate the Evolutionary Trace (ET) method's prediction of a conserved activation mechanism across family A 7TM receptors.

Main Methods:

  • Utilized Evolutionary Trace (ET) analysis to identify functionally important residue clusters by integrating evolutionary variation data with receptor structure.
  • Introduced six specific mutations targeting the predicted activation switch in the rat Angiotensin II (Ang II) type 1a receptor.
  • Assessed the impact of mutations on receptor activation through ligand binding, signaling pathway activation, and protein trafficking assays.

Main Results:

  • Mutations in the putative activation switch region of the AT1a receptor significantly altered its activation state.
  • Observed phenotypes included increased agonist affinity, elevated basal activity, promiscuous signaling, and constitutive receptor internalization.
  • The results highlight the importance of this residue patch in maintaining the receptor's inactive conformation.

Conclusions:

  • The identified residue patch plays a critical role in regulating 7TM receptor activation and maintaining the inactive state.
  • These findings support the hypothesis of a conserved activation switch mechanism common to family A 7TM receptors.
  • The study validates the utility of ET analysis in predicting functional elements within receptor superfamilies.