2y1x: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{STRUCTURE_2y1x|  PDB=2y1x  |  SCENE=  }}
-===CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1) IN COMPLEX WITH SINEFUNGIN AND INDOLE INHIBITOR===
-{{ABSTRACT_PUBMED_21410432}}
-==Function==
+==CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1) IN COMPLEX WITH SINEFUNGIN AND INDOLE INHIBITOR==
-[[http://www.uniprot.org/uniprot/CARM1_HUMAN CARM1_HUMAN]] 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 activate 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:16497732</ref> <ref>PMID:19405910</ref>
+<StructureSection load='2y1x' size='340' side='right'caption='[[2y1x]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2y1x]] 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=2Y1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y1X 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]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=845:N-(3-{5-[5-(1H-INDOL-4-YL)-1,3,4-OXADIAZOL-2-YL]-3-(TRIFLUOROMETHYL)-1H-PYRAZOL-1-YL}BENZYL)-L-ALANINAMIDE'>845</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=2y1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y1x OCA], [https://pdbe.org/2y1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y1x RCSB], [https://www.ebi.ac.uk/pdbsum/2y1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y1x ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CARM1_HUMAN CARM1_HUMAN] 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 activate 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:16497732</ref> <ref>PMID:19405910</ref>
-==About this Structure==
+==See Also==
-[[2y1x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y1X OCA].
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:021410432</ref><references group="xtra"/><references/>
+__TOC__
-[[Category: Histone-arginine N-methyltransferase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bandiera, T.]]
+[[Category: Large Structures]]
-[[Category: Bertrand, J A.]]
+[[Category: Bandiera T]]
-[[Category: Duke, G J.]]
+[[Category: Bertrand JA]]
-[[Category: Fasolini, M.]]
+[[Category: Duke GJ]]
-[[Category: Jayaraman, L.]]
+[[Category: Fasolini M]]
-[[Category: Kish, K F.]]
+[[Category: Jayaraman L]]
-[[Category: Klei, H E.]]
+[[Category: Kish KF]]
-[[Category: Purandare, A V.]]
+[[Category: Klei HE]]
-[[Category: Rosettani, P.]]
+[[Category: Purandare AV]]
-[[Category: Sack, J S.]]
+[[Category: Rosettani P]]
-[[Category: Thieffine, S.]]
+[[Category: Sack JS]]
-[[Category: Troiani, S.]]
+[[Category: Thieffine S]]
-[[Category: Xie, D.]]
+[[Category: Troiani S]]
-[[Category: Histone modification]]
+[[Category: Xie D]]
-[[Category: Transferase]]