The C-terminal region of the transcriptional regulator THAP11 forms a parallel coiled-coil domain involved in protein

Cyprian D Cukier1, Laurent Maveyraud1, Olivier Saurel1

  • 1Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, France.

Insights

Thanatos associated protein 11 (THAP11) is a key regulator of cell growth. This study reveals the first 3D structure of its C-terminal coiled-coil region, uncovering unusual dimeric features.

Area of Science:

  • Structural biology
  • Molecular biology
  • Cancer research

Background:

  • Thanatos associated protein 11 (THAP11) regulates cell cycle and growth, with differential expression in cancer.
  • THAP11 is a transcription factor with a unique zinc finger motif, but structural data for its variable regions are limited.

Purpose of the Study:

  • To determine the 3D structure of the C-terminal region of human THAP11.
  • To investigate the stability, dynamics, and oligomeric properties of this structure.

Main Methods:

  • X-ray crystallography
  • Molecular dynamics simulations
  • Biophysical experiments

Main Results:

  • The crystal structure of the THAP11 C-terminal region was determined.
  • This region forms a left-handed parallel homo-dimeric coiled-coil structure.
  • The structure exhibits several unusual characteristics compared to typical coiled-coils.

Conclusions:

  • The study provides the first 3D structural insights into a THAP family coiled-coil motif.
  • The findings elucidate the structural basis for THAP11's oligomeric properties and stability.
  • This work contributes to understanding THAP11's function in cellular processes and cancer.

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