2v7e

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(New page: 200px<br /> <applet load="2v7e" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v7e, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:2v7e.gif|left|200px]]<br />
 
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<applet load="2v7e" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2v7e, resolution 2.70&Aring;" />
 
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'''CRYSTAL STRUCTURE OF COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1), UNLIGANDED'''<br />
 
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==Overview==
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==Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), unliganded==
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Coactivator-associated arginine methyltransferase (CARM1) is a, transcriptional coactivator that methylates Arg17 and Arg26 in histone H3., CARM1 contains a conserved protein arginine methyltransferase (PRMT), catalytic core flanked by unique pre- and post-core regions. The crystal, structures of the CARM1 catalytic core in the apo and holo states reveal, cofactor-dependent formation of a substrate-binding groove providing a, specific access channel for arginine to the active site. The groove is, supported by the first eight residues of the post-core region, (C-extension), not present in other PRMTs. In vitro methylation assays, show that the C-extension is essential for all histone H3 methylation, activity, whereas the pre-core region is required for methylation of, Arg26, but not Arg17. ... [[http://ispc.weizmann.ac.il/pmbin/getpm?17882261 (full description)]]
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<StructureSection load='2v7e' size='340' side='right'caption='[[2v7e]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2v7e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V7E 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]] 2.7&#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=HG:MERCURY+(II)+ION'>HG</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=2v7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7e OCA], [https://pdbe.org/2v7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v7e RCSB], [https://www.ebi.ac.uk/pdbsum/2v7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v7e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CARM1_MOUSE CARM1_MOUSE] Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.<ref>PMID:10381882</ref> <ref>PMID:11341840</ref> <ref>PMID:11701890</ref> <ref>PMID:11713257</ref> <ref>PMID:11983685</ref> <ref>PMID:11997499</ref> <ref>PMID:12756295</ref> <ref>PMID:14966289</ref> <ref>PMID:15186775</ref> <ref>PMID:15616592</ref> <ref>PMID:16322096</ref> <ref>PMID:17218272</ref> <ref>PMID:17882261</ref> <ref>PMID:18188184</ref> <ref>PMID:19843527</ref> <ref>PMID:19897492</ref> <ref>PMID:21138967</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/v7/2v7e_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=2v7e 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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2V7E is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with HG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2V7E OCA]].
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase., Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH, EMBO J. 2007 Sep 20;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17882261 17882261]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Hassler M]]
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[[Category: Hassler, M.]]
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[[Category: Pearl LH]]
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[[Category: Pearl, L.H.]]
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[[Category: Roe SM]]
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[[Category: Roe, S.M.]]
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[[Category: Thompson-Vale V]]
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[[Category: Thompson-Vale, V.]]
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[[Category: Yue WW]]
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[[Category: Yue, W.W.]]
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[[Category: HG]]
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[[Category: alternative splicing]]
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[[Category: arginine methyltransferase]]
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[[Category: chromatin regulator]]
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[[Category: co- activator]]
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[[Category: cytoplasm]]
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[[Category: histone modification]]
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[[Category: methyltransferase]]
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[[Category: nucleus]]
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[[Category: s-adenosyl-l-methionine]]
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[[Category: transcription]]
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[[Category: transcription regulation]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 23:06:55 2007''
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Current revision

Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), unliganded

PDB ID 2v7e

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