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Neither Two-State nor Three-State: Dimerization of Lambda Cro Repressor.

John Yao, Jin Wang1

  • 1∥State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, People's Republic of China.

The Journal of Physical Chemistry Letters
|August 13, 2015
PubMed
Summary
This summary is machine-generated.

Lambda Cro repressor dimerization is explained by a new model, showing it starts with one folded and one unfolded monomer. This mechanism reconciles decades of debate on its two-state or three-state dimer structure.

Keywords:
all-atom structure-based modelcoupled binding-foldingfly castingfree energy landscapelambda cro repressorprotein dimerization

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Lambda Cro repressor is a well-studied dimeric transcription factor.
  • A long-standing debate exists regarding its two-state versus three-state dimerization mechanism.

Purpose of the Study:

  • To propose a novel mechanism model for Lambda Cro repressor dimerization.
  • To reconcile conflicting experimental findings on its structural states.

Main Methods:

  • All-atom structure-based simulations.
  • Computational modeling of protein-protein interactions.

Main Results:

  • The dimerization process initiates with one folded and one unfolded monomer.
  • Intrasubunit folding and intersubunit binding are partially coupled.
  • A 'fly casting' manner describes the interaction dynamics.

Conclusions:

  • The new model successfully reconciles previously conflicting experimental data.
  • Lambda Cro repressor dimerization involves a dynamic interplay between folding and binding.