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2gf7

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(New page: 200px<br /> <applet load="2gf7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gf7, resolution 2.200&Aring;" /> '''Double tudor domai...)
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[[Image:2gf7.gif|left|200px]]<br />
 
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<applet load="2gf7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2gf7, resolution 2.200&Aring;" />
 
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'''Double tudor domain structure'''<br />
 
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==Overview==
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==Double tudor domain structure==
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Biological responses to histone methylation critically depend on the, faithful readout and transduction of the methyl-lysine signal by, "effector" proteins, yet our understanding of methyl-lysine recognition, has so far been limited to the study of histone binding by chromodomain, and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc, domain-containing histone demethylase, binds methylated histone H3-K4 and, H4-K20. We found that the double tudor domain has an interdigitated, structure, and the unusual fold is required for its ability to bind, methylated histone tails. The cocrystal structure of the JMJD2A double, tudor domain with a trimethylated H3-K4 peptide reveals that the, trimethyl-K4 is bound in a cage of three aromatic residues, two of which, are from the tudor-2 motif, whereas the binding specificity is determined, by side-chain interactions involving amino acids from the tudor-1 motif., Our study provides mechanistic insights into recognition of methylated, histone tails by tudor domains and reveals the structural intricacy of, methyl-lysine recognition by two closely spaced effector domains.
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<StructureSection load='2gf7' size='340' side='right'caption='[[2gf7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2gf7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GF7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=SO4:SULFATE+ION'>SO4</scene></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=2gf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gf7 OCA], [https://pdbe.org/2gf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gf7 RCSB], [https://www.ebi.ac.uk/pdbsum/2gf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gf7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</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/gf/2gf7_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=2gf7 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2GF7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GF7 OCA].
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*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A., Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM, Science. 2006 May 5;312(5774):748-51. Epub 2006 Apr 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16601153 16601153]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bedford, M.T.]]
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[[Category: Bedford MT]]
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[[Category: Fang, J.]]
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[[Category: Fang J]]
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[[Category: Huang, Y.]]
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[[Category: Huang Y]]
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[[Category: Xu, R.M.]]
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[[Category: Xu RM]]
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[[Category: Zhang, Y.]]
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[[Category: Zhang Y]]
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[[Category: SO4]]
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[[Category: double tudor domain]]
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[[Category: jmjc domain containing]]
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[[Category: trimethyl hisone demethylase]]
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[[Category: trimethyl histone h3 lysine 4]]
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[[Category: tudor tandem]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:18:11 2007''
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Current revision

Double tudor domain structure

PDB ID 2gf7

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