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A Global Analysis of the Complex Structural Organization of KCTD Proteins and Their Functional Implications.

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Related Experiment Video

Updated: Apr 4, 2026

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
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KCTD5 is endowed with large, functionally relevant, interdomain motions.

Daniela Barone1,2, Nicole Balasco1,2, Luigi Vitagliano1

  • 1a Institute of Biostructures and Bioimaging, C.N.R. , Via Mezzocannone 16, Naples I-80134 , Italy.

Journal of Biomolecular Structure & Dynamics
|September 5, 2015
PubMed
Summary

KCTD5 protein

Keywords:
molecular dynamicsstructure–function relationshipssubstrate recognition domaintwistingubiquitination

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Dynamics

Background:

  • The KCTD protein family's functions are largely unknown.
  • KCTD5 is the only member with a defined 3D structure.

Purpose of the Study:

  • Investigate KCTD5's C-terminal domain (CTD) stability.
  • Analyze domain dynamics in full-length KCTD5.

Main Methods:

  • Utilized 120 ns Molecular Dynamics (MD) simulations.
  • Performed simulations on KCTD5's CTD and full-length protein.

Main Results:

  • KCTD5's CTD pentamer shows high intrinsic stability.
  • Identified exposed, potentially substrate-binding beta-strands.
  • Revealed a twisting motion between BTB and CTD domains, pivoted by Ser150.

Conclusions:

  • KCTD5's CTD is stable and may mediate substrate recognition.
  • Interdomain twisting is crucial for positioning substrates in ubiquitination machinery.