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

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• 作者：Cyprian D. Cukier ; ^{cyprian.cukier@gmx.com" class="auth_mail" title="E-mail the corresponding author} ; Laurent Maveyraud ; Olivier Saurel ; Valé ; rie Guillet ; Alain Milon ; Virginie Gervais ; ^{virginie.gervais@ipbs.fr" class="auth_mail" title="E-mail the corresponding author}
• 关键词：THAP ; Thanatos-associated protein ; HCF-1 ; host cell factor 1 ; HBM ; HCF-1 binding motif ; TEV ; tobacco etch virus ; LB ; Luria&ndash ; Bertani ; IPTG ; isopropyl-β-d-1-thiogalactopyranoside ; IMAC ; immobilized metal affinity chromatography ; SEC ; size exclusion chromatography ; DTT ; dithiothreitol ; MALS ; multiangle light scattering ; MD ; molecular dynamics ; CSI ; chemical shift index ; hetNOE ; 15N&ndash ; 1H heteronuclear NOE ; TRACT ; TROSY for rotational correlation times ; Kd ; dissociation constant ; RMSD ; root-
• 刊名：Journal of Structural Biology
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：194
• 期：3
• 页码：337-346
• 全文大小：2305 K

文摘

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.