2v7e

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[[Image:2v7e.gif|left|200px]]
 
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{{Structure
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==Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), unliganded==
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|PDB= 2v7e |SIZE=350|CAPTION= <scene name='initialview01'>2v7e</scene>, resolution 2.70&Aring;
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<StructureSection load='2v7e' size='340' side='right'caption='[[2v7e]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Hg+Binding+Site+For+Chain+B'>AC1</scene>, <scene name='pdbsite=AC2:Hg+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Hg+Binding+Site+For+Chain+A'>AC3</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>
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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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|ACTIVITY=
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=[[2v74|2V74]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7e OCA], [http://www.ebi.ac.uk/pdbsum/2v7e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v7e RCSB]</span>
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== Function ==
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}}
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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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'''CRYSTAL STRUCTURE OF COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1), UNLIGANDED'''
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==See Also==
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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. Kinetic analysis shows Arg17 methylation is potentiated by pre-acetylation of Lys18, and this is reflected in k(cat) rather than K(m). Together with the absence of specificity subsites in the structure, this suggests an electrostatic sensing mechanism for communicating the modification status of vicinal residues as part of the syntax of the 'histone code.'
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2V7E is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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 Oct 17;26(20):4402-12. Epub 2007 Sep 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17882261 17882261]
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[[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: 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://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:10 2008''
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Current revision

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

PDB ID 2v7e

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