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1z60

From Proteopedia

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[[Image:1z60.png|left|200px]]
 
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==Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit==
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The line below this paragraph, containing "STRUCTURE_1z60", creates the "Structure Box" on the page.
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<StructureSection load='1z60' size='340' side='right'caption='[[1z60]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1z60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e53 1e53]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z60 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1z60| PDB=1z60 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z60 OCA], [https://pdbe.org/1z60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z60 RCSB], [https://www.ebi.ac.uk/pdbsum/1z60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z60 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TF2H2_HUMAN TF2H2_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. The N-terminus interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z6/1z60_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1z60 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human general transcription factor TFIIH is involved in both transcription and DNA nucleotide excision repair. Among the 10 subunits of the complex, p44 subunit plays a crucial role in both mechanisms. Its N-terminal domain interacts with the XPD helicase, whereas its C-terminal domain is involved specifically in the promoter escape activity. By mutating an exposed and non-conserved cysteine residue into a serine, we produced a soluble mutant of p44-(321-395) suitable for solution structure determination. The domain adopts a C4C4 RING domain structure with sequential organization of beta-strands that is related to canonical RING domains by a circular permutation of the beta-sheet elements. Analysis of the molecular surface and mutagenesis experiments suggests that the binding of p44-(321-395) to TFIIH p34 subunit is not mediated by electrostatic interactions and, thus, differs from previously reported interaction mechanisms involving RING domains.
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===Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit===
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Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions.,Kellenberger E, Dominguez C, Fribourg S, Wasielewski E, Moras D, Poterszman A, Boelens R, Kieffer B J Biol Chem. 2005 May 27;280(21):20785-92. Epub 2005 Mar 24. PMID:15790571<ref>PMID:15790571</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15790571}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1z60" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15790571 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15790571}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1z60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e53 1e53]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z60 OCA].
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==Reference==
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<ref group="xtra">PMID:15790571</ref><ref group="xtra">PMID:10882739</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Boelens, R.]]
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[[Category: Large Structures]]
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[[Category: Dominguez, C.]]
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[[Category: Boelens R]]
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[[Category: Fribourg, S.]]
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[[Category: Dominguez C]]
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[[Category: Kellenberger, E.]]
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[[Category: Fribourg S]]
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[[Category: Kieffer, B.]]
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[[Category: Kellenberger E]]
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[[Category: Moras, D.]]
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[[Category: Kieffer B]]
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[[Category: Poterszman, A.]]
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[[Category: Moras D]]
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[[Category: Wasielewski, E.]]
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[[Category: Poterszman A]]
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[[Category: Basic transcription factor]]
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[[Category: Wasielewski E]]
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[[Category: Ring finger]]
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[[Category: Zinc binding protein]]
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Current revision

Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit

PDB ID 1z60

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