2v74

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2v74" [edit=sysop:move=sysop])
Current revision (09:35, 14 February 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2v74.png|left|200px]]
 
-
{{STRUCTURE_2v74| PDB=2v74 | SCENE= }}
+
==Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), in complex with S-adenosyl-homocysteine==
 +
<StructureSection load='2v74' size='340' side='right'caption='[[2v74]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2v74]] 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=2V74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V74 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]] 2.7&#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=2v74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v74 OCA], [https://pdbe.org/2v74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v74 RCSB], [https://www.ebi.ac.uk/pdbsum/2v74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v74 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>
 +
== 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/v7/2v74_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=2v74 ConSurf].
 +
<div style="clear:both"></div>
-
===CRYSTAL STRUCTURE OF COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1), IN COMPLEX WITH S-ADENOSYL-HOMOCYSTEINE===
+
==See Also==
-
 
+
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
-
{{ABSTRACT_PUBMED_17882261}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[2v74]] is a 4 chain structure with 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=2V74 OCA].
+
</StructureSection>
-
 
+
[[Category: Large Structures]]
-
==Reference==
+
-
<ref group="xtra">PMID:017882261</ref><references group="xtra"/>
+
-
[[Category: Histone-arginine N-methyltransferase]]
+
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Hassler, M.]]
+
[[Category: Hassler M]]
-
[[Category: Pearl, L H.]]
+
[[Category: Pearl LH]]
-
[[Category: Roe, S M.]]
+
[[Category: Roe SM]]
-
[[Category: Thompson-Vale, V.]]
+
[[Category: Thompson-Vale V]]
-
[[Category: Yue, W W.]]
+
[[Category: Yue WW]]
-
[[Category: Arginine methyltransferase]]
+
-
[[Category: Chromatin regulator]]
+
-
[[Category: Co- activator]]
+
-
[[Category: Histone modification]]
+
-
[[Category: Methyltransferase]]
+
-
[[Category: Nucleus]]
+
-
[[Category: S-adenosyl-l-methionine]]
+
-
[[Category: Transcription]]
+
-
[[Category: Transcription regulation]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), in complex with S-adenosyl-homocysteine

PDB ID 2v74

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools