5AJS

Crystal structure of a coiled-coil domain from human THAP11

Summary for 5AJS

• Entry DOI: 10.2210/pdb5ajs/pdb
• Descriptor: THAP DOMAIN-CONTAINING PROTEIN 11 (2 entities in total)
• Functional Keywords: transcription, transcription factor
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 4
• Total formula weight: 32030.15

Authors

Cukier, C.D.,Maveyraud, L.,Milon, A.,Gervais, V. (deposition date: 2015-02-27, release date: 2016-03-09, Last modification date: 2024-01-10)

Primary citation

Cukier, C.D.,Maveyraud, L.,Saurel, O.,Guillet, V.,Milon, A.,Gervais, V.
The C-Terminal Region of the Transcriptional Regulator Thap11 Forms a Parallel Coiled-Coil Domain Involved in Protein Dimerization.
J.Struct.Biol., 194:337-, 2016

PubMed 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.

PubMed: 26975212
DOI: 10.1016/J.JSB.2016.03.010

Experimental method

X-RAY DIFFRACTION (2.3 Å)