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Transient disorder: Calcineurin as an example.

Trevor P Creamer1

  • 1Center for Structural Biology; Department of Molecular and Cellular Biochemistry; University of Kentucky; Lexington, KY USA.

Intrinsically Disordered Proteins
|May 19, 2017
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins evade degradation by transiently folding upon binding partners. Calmodulin binding to calcineurin involves a transiently disordered regulatory domain, facilitating rapid activation via a "catch and release" mechanism.

Keywords:
calmodulinchaperonesdegradationintrinsically disordered regionmisfoldingphosphataseproteases

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Dynamics

Background:

  • Intrinsically disordered proteins (IDPs) pose a challenge to cellular degradation machinery.
  • Understanding how IDPs evade degradation is crucial for cellular regulation.

Purpose of the Study:

  • To investigate the role of transient disorder in protein-protein interactions.
  • To elucidate the activation mechanism of calcineurin by calmodulin.

Main Methods:

  • Review of 30 years of studies on calmodulin-calcineurin interactions.
  • Analysis of protein conformational changes during activation.

Main Results:

  • The regulatory domain of calcineurin exhibits transient disorder during calmodulin binding.
  • This transiently disordered state is a critical intermediate facilitating rapid calmodulin binding.
  • The activation/deactivation cycle of calcineurin by calmodulin can be described as a "catch and release" mechanism.

Conclusions:

  • Transient disorder is a key mechanism for IDPs to evade degradation.
  • Calcineurin's activation by calmodulin exemplifies a "catch and release" process involving transient protein disorder.