5k8x
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of mouse CARM1 in complex with inhibitor U3== | |
- | + | <StructureSection load='5k8x' size='340' side='right' caption='[[5k8x]], [[Resolution|resolution]] 1.99Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5k8x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K8X FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6ZH:[[[(~{E})-3-[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]prop-2-enyl]amino]-azanyl-methylidene]azanium'>6ZH</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=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | |
- | [[Category: | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> |
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_I_protein_arginine_methyltransferase Type I protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.319 2.1.1.319] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k8x OCA], [http://pdbe.org/5k8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k8x RCSB], [http://www.ebi.ac.uk/pdbsum/5k8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k8x ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Lk3 transgenic mice]] | ||
+ | [[Category: Type I protein arginine methyltransferase]] | ||
+ | [[Category: Bonnefond, L]] | ||
+ | [[Category: Cavarelli, J]] | ||
+ | [[Category: Cura, V]] | ||
+ | [[Category: Hassenboehler, P]] | ||
[[Category: Mailliot, J]] | [[Category: Mailliot, J]] | ||
- | [[Category: | + | [[Category: Marechal, N]] |
[[Category: Troffer-Charlier, N]] | [[Category: Troffer-Charlier, N]] | ||
- | [[Category: | + | [[Category: Wurtz, J M]] |
- | [[Category: | + | [[Category: Catalytic domain]] |
- | [[Category: | + | [[Category: Chromatin regulator]] |
- | [[Category: | + | [[Category: Mrna processing]] |
- | [[Category: | + | [[Category: Mrna splicing]] |
+ | [[Category: Nucleus]] | ||
+ | [[Category: Protein arginine methyltransferase]] | ||
+ | [[Category: S-adenosyl-l-methionine]] | ||
+ | [[Category: Transcription]] | ||
+ | [[Category: Transcription regulation]] | ||
+ | [[Category: Transferase]] |
Revision as of 08:35, 16 November 2017
Crystal structure of mouse CARM1 in complex with inhibitor U3
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Categories: Lk3 transgenic mice | Type I protein arginine methyltransferase | Bonnefond, L | Cavarelli, J | Cura, V | Hassenboehler, P | Mailliot, J | Marechal, N | Troffer-Charlier, N | Wurtz, J M | Catalytic domain | Chromatin regulator | Mrna processing | Mrna splicing | Nucleus | Protein arginine methyltransferase | S-adenosyl-l-methionine | Transcription | Transcription regulation | Transferase