3b3f: Difference between revisions

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-[[Image:3b3f.gif|left|200px]]<br /><applet load="3b3f" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="3b3f, resolution 2.20&Aring;" />
-'''The 2.2 A crystal structure of the catalytic domain of coactivator-associated arginine methyl transferase I(CARM1,142-478), in complex with S-adenosyl homocysteine'''<br />
-==Overview==
+==The 2.2 A crystal structure of the catalytic domain of coactivator-associated arginine methyl transferase I(CARM1,142-478), in complex with S-adenosyl homocysteine==
-Coactivator-associated arginine methyltransferase 1 (CARM1), a protein, arginine methyltransferase recruited by several transcription factors, methylates a large variety of proteins and plays a critical role in gene, expression. We report, in this paper, four crystal structures of isolated, modules of CARM1. The 1.7 A crystal structure of the N-terminal domain of, CARM1 reveals an unexpected PH domain, a scaffold frequently found to, regulate protein-protein interactions in a large variety of biological, processes. Three crystal structures of the CARM1 catalytic module, two, free and one cofactor-bound forms (refined at 2.55 A, 2.4 A and 2.2 A, respectively) reveal large structural modifications including disorder to, order transition, helix to strand transition and active site, modifications. The N-terminal and the C-terminal end of CARM1 catalytic, module contain molecular switches that may inspire how CARM1 regulates its, biological activities by protein-protein interactions.
+<StructureSection load='3b3f' size='340' side='right'caption='[[3b3f]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3b3f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B3F 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]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3b3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b3f OCA], [https://pdbe.org/3b3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b3f RCSB], [https://www.ebi.ac.uk/pdbsum/3b3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b3f ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CARM1_RAT CARM1_RAT] 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:15944154</ref>   Isoform 3 specifically affects pre-mRNA splicing. This activity is independent from methyltransferase activity.<ref>PMID:15944154</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/3b3f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3b3f ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-B3F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B3F OCA].
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains., Troffer-Charlier N, Cura V, Hassenboehler P, Moras D, Cavarelli J, EMBO J. 2007 Oct 17;26(20):4391-401. Epub 2007 Sep 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17882262 17882262]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Cavarelli J]]
-[[Category: Cavarelli, J.]]
+[[Category: Cura V]]
-[[Category: Cura, V.]]
+[[Category: Hassenboehler P]]
-[[Category: Hassenboehler, P.]]
+[[Category: Moras D]]
-[[Category: Moras, D.]]
+[[Category: Troffer-Charlier N]]
-[[Category: Troffer-Charlier, N.]]
-[[Category: SAH]]
-[[Category: alternative splicing]]
-[[Category: catalytic domain]]
-[[Category: chromatin regulator]]
-[[Category: cytoplasm]]
-[[Category: mrna processing]]
-[[Category: mrna splicing]]
-[[Category: nucleus]]
-[[Category: protein arginine methyltransferase]]
-[[Category: s-adenosyl-l-methionine]]
-[[Category: transcription]]
-[[Category: transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:30:02 2008''