2gd7

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{{Seed}}
 
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[[Image:2gd7.png|left|200px]]
 
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==The Structure of the Cyclin T-binding domain of Hexim1 reveals the molecular basis for regulation of transcription elongation==
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The line below this paragraph, containing "STRUCTURE_2gd7", creates the "Structure Box" on the page.
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<StructureSection load='2gd7' size='340' side='right'caption='[[2gd7]]' 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'>[[2gd7]] is a 2 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=2GD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GD7 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gd7 OCA], [https://pdbe.org/2gd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gd7 RCSB], [https://www.ebi.ac.uk/pdbsum/2gd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gd7 ProSAT]</span></td></tr>
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{{STRUCTURE_2gd7| PDB=2gd7 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HEXI1_HUMAN HEXI1_HUMAN] Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity.<ref>PMID:12941847</ref> <ref>PMID:12581153</ref> <ref>PMID:14580347</ref> <ref>PMID:12832472</ref> <ref>PMID:15201869</ref> <ref>PMID:15713661</ref> <ref>PMID:15940264</ref> <ref>PMID:15941832</ref> <ref>PMID:17088550</ref>
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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/gd/2gd7_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=2gd7 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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Hexim1 is a cellular protein that associates with the positive transcription elongation factor b (P-TEFb) to regulate RNA polymerase II elongation of nascent mRNA transcripts. It directly binds to Cyclin T1 of P-TEFb and inhibits the kinase activity of Cdk9, leading to an arrest of transcription elongation. Here, we report the solution structure of the Cyclin T binding domain (TBD) of Hexim1 that forms a parallel coiled-coil homodimer composed of two segments and a preceding alpha helix that folds back onto the first coiled-coil unit. NMR titration, fluorescence, and immunoprecipitation experiments revealed the binding interface to Cyclin T1, which covers a large surface on the first coiled-coil segment. Electrostatic interactions between an acidic patch on Hexim1 and positively charged residues of Cyclin T1 drive the complex formation that is confirmed by mutagenesis data on Hexim1 mediated transcription regulation in cells. Thus, our studies provide structural insights how Hexim1 recognizes the Cyclin T1 subunit of P-TEFb, which is a key step toward the regulation of transcription elongation.
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===The Structure of the Cyclin T-binding domain of Hexim1 reveals the molecular basis for regulation of transcription elongation===
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Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb.,Dames SA, Schonichen A, Schulte A, Barboric M, Peterlin BM, Grzesiek S, Geyer M Proc Natl Acad Sci U S A. 2007 Sep 4;104(36):14312-7. Epub 2007 Aug 27. PMID:17724342<ref>PMID:17724342</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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The line below this paragraph, {{ABSTRACT_PUBMED_17724342}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2gd7" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17724342 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17724342}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2GD7 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GD7 OCA].
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==Reference==
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<ref group="xtra">PMID:17724342</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Dames, S A.]]
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[[Category: Large Structures]]
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[[Category: Clp-1]]
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[[Category: Dames SA]]
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[[Category: Coiled coil]]
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[[Category: Edg1]]
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[[Category: Hexim1]]
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[[Category: Maq1]]
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[[Category: P-tefb nmr]]
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[[Category: Positive transcription elongation factor-b]]
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[[Category: Structure determination]]
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[[Category: Symmetric dimer]]
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[[Category: Transcription elongation]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:11:54 2009''
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Current revision

The Structure of the Cyclin T-binding domain of Hexim1 reveals the molecular basis for regulation of transcription elongation

PDB ID 2gd7

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