5isc: Difference between revisions

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-'''Unreleased structure'''
-The entry 5isc is ON HOLD  until Paper Publication
+==Crystal structure of mouse CARM1 in complex with inhibitor SA0491==
+<StructureSection load='5isc' size='340' side='right'caption='[[5isc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5isc]] is a 4 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=5ISC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ISC FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6D0:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](3-BROMO-2-OXOPROPYL)AMINO}-5-DEOXYADENOSINE'>6D0</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene>, <scene name='pdbligand=SAO:5-S-[(3S)-3-AZANIUMYL-3-CARBOXYPROPYL]-5-THIOADENOSINE'>SAO</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5isc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isc OCA], [https://pdbe.org/5isc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5isc RCSB], [https://www.ebi.ac.uk/pdbsum/5isc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5isc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
-Authors: Cura, V., Marechal, N., Mailliot, J., Troffer-Charlier, N., Hassenboehler, P., Wurtz, J.M., Bonnefond, L., Cavarelli, J.
+==See Also==
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
-Description: Crystal structure of mouse CARM1 in complex with inhibitor SA0491
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Mailliot, J]]
+__TOC__
-[[Category: Cavarelli, J]]
+</StructureSection>
-[[Category: Bonnefond, L]]
+[[Category: Large Structures]]
-[[Category: Marechal, N]]
+[[Category: Mus musculus]]
-[[Category: Wurtz, J.M]]
+[[Category: Bonnefond L]]
-[[Category: Hassenboehler, P]]
+[[Category: Cavarelli J]]
-[[Category: Cura, V]]
+[[Category: Cura V]]
-[[Category: Troffer-Charlier, N]]
+[[Category: Hassenboehler P]]
+[[Category: Mailliot J]]
+[[Category: Marechal N]]
+[[Category: Troffer-Charlier N]]
+[[Category: Wurtz JM]]