Related Experiment Video
Updated: Mar 24, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
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.
Abstract:
Thanatos associated protein 11 (THAP11) is a cell cycle and cell growth regulator differentially expressed in cancer cells. THAP11 belongs to a distinct family of transcription factors recognizing specific DNA sequences via an atypical zinc finger motif and regulating diverse cellular processes. Outside the extensively characterized DNA-binding domain, THAP proteins vary in size and predicted domains, for which structural data are still lacking. We report here the crystal structure of the C-terminal region of human THAP11 protein, providing the first 3D structure of a coiled-coil motif from a THAP family member. We further investigate the stability, dynamics and oligomeric properties of the determined structure combining molecular dynamics simulations and biophysical experiments. Our results show that the C-ter region of THAP11 forms a left-handed parallel homo-dimeric coiled-coil structure possessing several unusual features.
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.
More Related Videos
07:08Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
13:02Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
Published on: December 28, 2019
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Cytoskeletal Linker Proteins - Plakins