View source for 5ajs


==Crystal structure of a coiled-coil domain from human THAP11==
<StructureSection load='5ajs' size='340' side='right'caption='[[5ajs]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ajs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AJS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ajs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ajs OCA], [https://pdbe.org/5ajs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ajs RCSB], [https://www.ebi.ac.uk/pdbsum/5ajs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ajs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THA11_HUMAN THA11_HUMAN] Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

The C-terminal region of the transcriptional regulator THAP11 forms a parallel coiled-coil domain involved in protein dimerization.,Cukier CD, Maveyraud L, Saurel O, Guillet V, Milon A, Gervais V J Struct Biol. 2016 Jun;194(3):337-46. doi: 10.1016/j.jsb.2016.03.010. Epub 2016 , Mar 11. PMID:26975212<ref>PMID:26975212</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ajs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cukier CD]]
[[Category: Gervais V]]
[[Category: Maveyraud L]]
[[Category: Milon A]]