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Related Experiment Videos

Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control

H E Parge1, A S Arvai, D J Murtari

  • 1The Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.

Science (New York, N.Y.)
|October 15, 1993
PubMed
Summary
This summary is machine-generated.

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The cell cycle protein CksHs2 forms an unexpected hexamer structure. This structure may act as a central hub for cyclin-dependent kinases (Cdk

Area of Science:

  • Structural biology
  • Molecular cell biology
  • Protein biochemistry

Background:

  • The cell cycle regulatory protein CksHs2 is crucial for cyclin-dependent kinases (Cdk's) function.
  • Understanding CksHs2's structure is key to elucidating its role in cell cycle control.

Purpose of the Study:

  • To determine the crystal structure of the CksHs2 protein.
  • To investigate the structural basis for CksHs2's interaction with Cdks.

Main Methods:

  • X-ray crystallography at 2.1 A resolution.
  • Structural analysis of protein assembly and conserved regions.

Main Results:

  • The CksHs2 protein forms an unexpected hexameric structure.
  • This hexamer features an unusual 12-stranded beta barrel fold with interlocked dimers.

Related Experiment Videos

  • Conserved regions mediate beta strand exchange, metal/anion binding, and form a central tunnel lined by charged helices.

    • Conclusions:

    • The CksHs2 hexamer structure may serve as a prototype for this protein class.
    • The structure accommodates multiple Cdk subunits, suggesting a role as a multimerization hub in cell cycle regulation.