5nus: Difference between revisions
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==Structure of a minimal complex between p44 and p34 from Chaetomium thermophilum== | |||
<StructureSection load='5nus' size='340' side='right' caption='[[5nus]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nus]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NUS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nus OCA], [http://pdbe.org/5nus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nus RCSB], [http://www.ebi.ac.uk/pdbsum/5nus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nus ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The general transcription factor IIH (TFIIH) is a multi-protein complex and its 10 subunits are engaged in an intricate protein-protein interaction network critical for the regulation of its transcription and DNA repair activities that are so far little understood on a molecular level. In this study, we focused on the p44 and the p34 subunits, which are central for the structural integrity of core-TFIIH. We solved crystal structures of a complex formed by the p34 N-terminal vWA and p44 C-terminal zinc binding domains from Chaetomium thermophilum and from Homo sapiens. Intriguingly, our functional analyses clearly revealed the presence of a second interface located in the C-terminal zinc binding region of p34, which can rescue a disrupted interaction between the p34 vWA and the p44 RING domain. In addition, we demonstrate that the C-terminal zinc binding domain of p34 assumes a central role with respect to the stability and function of TFIIH. Our data reveal a redundant interaction network within core-TFIIH, which may serve to minimize the susceptibility to mutational impairment. This provides first insights why so far no mutations in the p34 or p44 TFIIH-core subunits have been identified that would lead to the hallmark nucleotide excision repair syndromes xeroderma pigmentosum or trichothiodystrophy. | |||
The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH.,Radu L, Schoenwetter E, Braun C, Marcoux J, Koelmel W, Schmitt DR, Kuper J, Cianferani S, Egly JM, Poterszman A, Kisker C Nucleic Acids Res. 2017 Aug 25. doi: 10.1093/nar/gkx743. PMID:28977422<ref>PMID:28977422</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5nus" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kisker, C]] | |||
[[Category: Koelmel, W]] | |||
[[Category: Kuper, J]] | |||
[[Category: Schmitt, D R]] | |||
[[Category: Schoenwetter, E]] | |||
[[Category: Ring finger domain]] | |||
[[Category: Transcription]] | |||
[[Category: Von willebrand factor a like]] | |||
Revision as of 07:02, 18 October 2017
Structure of a minimal complex between p44 and p34 from Chaetomium thermophilum
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