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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Dynamics-Driven Allostery in Protein Kinases.

Alexandr P Kornev1, Susan S Taylor2

  • 1Department of Pharmacology, University of California at San Diego, La Jolla, CA, 92093, USA.

Trends in Biochemical Sciences
|October 21, 2015
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Summary

Protein kinases

Keywords:
allosterycommunity analysisprotein dynamicsprotein kinases

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Area of Science:

  • Biochemistry and structural biology, focusing on protein dynamics.

Background:

  • Protein kinase functionality is intrinsically linked to their dynamic structural states.
  • Understanding these dynamics is crucial for comprehending kinase regulation.

Purpose of the Study:

  • To elucidate the dynamic organization of active protein kinases.
  • To investigate the role of dynamic communities and hydrophobic spines in kinase allosteric regulation.

Main Methods:

  • Analysis of protein kinase structures and dynamics.
  • Identification of residue-based dynamic communities and their temporal behavior (μs-ms timescale).

Main Results:

  • Active kinases exhibit dynamic patterns with semirigid residue communities.
  • Hydrophobic spines connect these communities, independent of traditional structural elements.
  • Community integration relies on hydrophobic spine assembly and activation loop phosphorylation.
  • Single mutations disrupt this dynamic infrastructure, impacting allosteric signaling.

Conclusions:

  • Protein kinase allosteric regulation is fundamentally driven by molecular dynamics.
  • The identified dynamic communities and their organization provide a new framework for understanding kinase function.