1pfj
From Proteopedia
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| - | [[Image:1pfj.gif|left|200px]] | ||
| - | + | ==Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit== | |
| - | + | <StructureSection load='1pfj' size='340' side='right'caption='[[1pfj]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1pfj]] 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=1PFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PFJ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1pfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfj OCA], [https://pdbe.org/1pfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfj RCSB], [https://www.ebi.ac.uk/pdbsum/1pfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfj 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. | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pf/1pfj_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pfj ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The human general transcription factor TFIIH is involved in both transcription and DNA repair. We have identified a structural domain in the core subunit of TFIIH, p62, which is absolutely required for DNA repair activity through the nucleotide excision repair pathway. Using coimmunoprecipitation experiments, we showed that this activity involves the interaction between the N-terminal domain of p62 and the 3' endonuclease XPG, a major component of the nucleotide excision repair machinery. Furthermore, we reconstituted a functional TFIIH particle with a mutant of p62 lacking the N-terminal domain, showing that this domain is not required for assembly of the TFIIH complex and basal transcription. We solved its three-dimensional structure and found an unpredicted pleckstrin homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new class of activity for this fold. | The human general transcription factor TFIIH is involved in both transcription and DNA repair. We have identified a structural domain in the core subunit of TFIIH, p62, which is absolutely required for DNA repair activity through the nucleotide excision repair pathway. Using coimmunoprecipitation experiments, we showed that this activity involves the interaction between the N-terminal domain of p62 and the 3' endonuclease XPG, a major component of the nucleotide excision repair machinery. Furthermore, we reconstituted a functional TFIIH particle with a mutant of p62 lacking the N-terminal domain, showing that this domain is not required for assembly of the TFIIH complex and basal transcription. We solved its three-dimensional structure and found an unpredicted pleckstrin homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new class of activity for this fold. | ||
| - | + | TFIIH contains a PH domain involved in DNA nucleotide excision repair.,Gervais V, Lamour V, Jawhari A, Frindel F, Wasielewski E, Dubaele S, Egly JM, Thierry JC, Kieffer B, Poterszman A Nat Struct Mol Biol. 2004 Jul;11(7):616-22. Epub 2004 Jun 13. PMID:15195146<ref>PMID:15195146</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1pfj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Frindel | + | [[Category: Frindel F]] |
| - | [[Category: Gervais | + | [[Category: Gervais V]] |
| - | [[Category: Jawhari | + | [[Category: Jawhari A]] |
| - | [[Category: Kieffer | + | [[Category: Kieffer B]] |
| - | [[Category: Lamour | + | [[Category: Lamour V]] |
| - | [[Category: Poterszman | + | [[Category: Poterszman A]] |
| - | + | [[Category: Thierry JC]] | |
| - | [[Category: Thierry | + | [[Category: Wasielewski E]] |
| - | [[Category: Wasielewski | + | |
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Current revision
Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit
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