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Updated: Jan 13, 2026

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Intrinsic conformational equilibria position arrestin-2 for activation.

Tucker J Shriver1, Kerem Kahraman1, Mingzhe Pan2

  • 1Department of Pharmacology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.

Biorxiv : the Preprint Server for Biology
|January 9, 2026
PubMed
Summary
This summary is machine-generated.

Arrestin-2 intrinsically samples activation-ready states before binding partners. This research defines the solution-state equilibria governing arrestin pre-activation and signaling competence.

Keywords:
GPCR signaling adaptorbeta-arrestinconformational equilibriadynamicsinterdomain rotationpre-activationthermodynamics of activation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Arrestins regulate G protein-coupled receptor (GPCR) signaling through conformational changes.
  • The solution-state equilibria governing arrestin pre-activation are not well understood.

Purpose of the Study:

  • To characterize the intrinsic conformational landscape of full-length human arrestin-2 in solution.
  • To define the solution-state equilibria underlying arrestin pre-activation.

Main Methods:

  • Methyl-specific nuclear magnetic resonance (NMR) spectroscopy.
  • Temperature-dependent chemical shift analysis.
  • Relaxation measurements.

Main Results:

  • Identified two distinct equilibria with separable thermodynamic and kinetic signatures.
  • A slow, enthalpically-favored process populates an active-like conformation at physiological temperatures.
  • A faster equilibrium involves C-terminal tail release with opposing thermodynamic behavior.

Conclusions:

  • Arrestin-2 intrinsically samples activation-relevant conformations without binding partners.
  • Provides a solution-state framework for arrestin pre-activation and signaling competence.