7bul: Difference between revisions
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==Solution structure of the tandem PH and BSD1 domains of TFIIH p62== | |||
<StructureSection load='7bul' size='340' side='right'caption='[[7bul]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7bul]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BUL FirstGlance]. <br> | |||
</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=7bul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bul OCA], [https://pdbe.org/7bul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bul RCSB], [https://www.ebi.ac.uk/pdbsum/7bul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bul ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TF2H1_HUMAN TF2H1_HUMAN] Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
TFIIH is a crucial transcription and DNA repair factor consisting of the seven-subunit core. The core subunit p62 contains a pleckstrin homology domain (PH-D), which is essential for locating TFIIH at transcription initiation and DNA damage sites, and two BSD (BTF2-like transcription factors, synapse-associated proteins and DOS2-like proteins) domains. A recent cryo-electron microscopy (cryo-EM) structure of human TFIIH visualized most parts of core, except for the PH-D. Here, by nuclear magnetic resonance spectroscopy we have established the solution structure of human p62 PH-D connected to the BSD1 domain by a highly flexible linker, suggesting the flexibility of PH-D in TFIIH. Based on this dynamic character, the PH-D was modeled in the cryo-EM structure to obtain the whole human TFIIH core structure, which indicates that the PH-D moves around the surface of core with a specific but limited spatial distribution; these dynamic structures were refined by molecular dynamics (MD) simulations. Furthermore, we built models, also refined by MD simulations, of TFIIH in complex with five p62-binding partners, including transcription factors TFIIEalpha, p53 and DP1, and nucleotide excision repair factors XPC and UVSSA. The models explain why the PH-D is crucially targeted by these factors, which use their intrinsically disordered acidic regions for TFIIH recruitment. | |||
Structural and dynamical insights into the PH domain of p62 in human TFIIH.,Okuda M, Ekimoto T, Kurita JI, Ikeguchi M, Nishimura Y Nucleic Acids Res. 2020 Nov 19. pii: 5992292. doi: 10.1093/nar/gkaa1045. PMID:33211877<ref>PMID:33211877</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7bul" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Nishimura Y]] | |||
[[Category: Okuda M]] | |||
