2kis

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{{Seed}}
 
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[[Image:2kis.png|left|200px]]
 
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==Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker==
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The line below this paragraph, containing "STRUCTURE_2kis", creates the "Structure Box" on the page.
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<StructureSection load='2kis' size='340' side='right'caption='[[2kis]]' 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'>[[2kis]] 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=2KIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KIS 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=2kis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kis OCA], [https://pdbe.org/2kis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kis RCSB], [https://www.ebi.ac.uk/pdbsum/2kis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kis ProSAT]</span></td></tr>
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{{STRUCTURE_2kis| PDB=2kis | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TCRG1_HUMAN TCRG1_HUMAN] Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.<ref>PMID:9315662</ref> <ref>PMID:11604498</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/ki/2kis_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=2kis 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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FF domains are poorly understood protein interaction modules that are present within eukaryotic transcription factors, such as CA150 (TCERG-1). The CA150 FF domains have been shown to mediate interactions with the phosphorylated C-terminal domain of RNA polymerase II (phosphoCTD) and a multitude of transcription factors and RNA processing proteins, and may therefore have a central role in organizing transcription. FF domains occur in tandem arrays of up to six domains, although it is not known whether they adopt higher-order structures. We have used the CA150 FF1+FF2 domains as a model system to examine whether tandem FF domains form higher-order structures in solution using NMR spectroscopy. In the solution structure of FF1 fused to the linker that joins FF1 to FF2, we observed that the highly conserved linker peptide is ordered and forms a helical extension of helix alpha3, suggesting that the interdomain linker might have a role in orientating FF1 relative to FF2. However, examination of the FF1+FF2 domains using relaxation NMR experiments revealed that although these domains are not rigidly orientated relative to one another, they do not tumble independently. Thus, the FF1+FF2 structure conforms to a dumbbell-shape in solution, where the helical interdomain linker maintains distance between the two dynamic FF domains without cementing their relative orientations. This model for FF domain organization within tandem arrays suggests a general mechanism by which individual FF domains can manoeuvre to achieve optimal recognition of flexible binding partners, such as the intrinsically-disordered phosphoCTD.
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===Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker===
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Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays.,Murphy JM, Hansen DF, Wiesner S, Muhandiram DR, Borg M, Smith MJ, Sicheri F, Kay LE, Forman-Kay JD, Pawson T J Mol Biol. 2009 Oct 23;393(2):409-24. Epub 2009 Aug 26. PMID:19715701<ref>PMID:19715701</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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<div class="pdbe-citations 2kis" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19715701}}, adds the Publication Abstract to the page
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19715701 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19715701}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2KIS is a 1 chain structure of sequence 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=2KIS OCA].
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==Reference==
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<ref group="xtra">PMID:19715701</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Borg, M.]]
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[[Category: Large Structures]]
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[[Category: Forman-Kay, J D.]]
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[[Category: Borg M]]
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[[Category: Hansen, D.]]
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[[Category: Forman-Kay JD]]
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[[Category: Kay, L E.]]
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[[Category: Hansen D]]
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[[Category: Muhandiram, D.]]
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[[Category: Kay LE]]
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[[Category: Murphy, J M.]]
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[[Category: Muhandiram D]]
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[[Category: Pawson, T.]]
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[[Category: Murphy JM]]
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[[Category: Sicheri, F.]]
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[[Category: Pawson T]]
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[[Category: Smith, M J.]]
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[[Category: Sicheri F]]
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[[Category: Wiesner, S.]]
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[[Category: Smith MJ]]
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[[Category: Activator]]
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[[Category: Wiesner S]]
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[[Category: Alternative splicing]]
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[[Category: Coiled coil]]
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[[Category: Extended helix]]
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[[Category: Ff domain]]
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[[Category: Interdomain dynamic]]
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[[Category: Interdomain helix]]
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[[Category: Linker peptide]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Repressor]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transcription regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 21 09:42:17 2009''
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Current revision

Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker

PDB ID 2kis

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