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2oqb

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[[Image:2oqb.png|left|200px]]
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==Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)==
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<StructureSection load='2oqb' size='340' side='right' caption='[[2oqb]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2oqb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OQB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<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=10116 Rattus norvegicus])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-arginine_N-methyltransferase Histone-arginine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125] </span></td></tr>
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<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=2oqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2oqb RCSB], [http://www.ebi.ac.uk/pdbsum/2oqb PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2oqb| PDB=2oqb | SCENE= }}
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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:17882262<ref>PMID:17882262</ref>
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===Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_17882262}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2oqb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQB OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:017882262</ref><references group="xtra"/>
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[[Category: Histone-arginine N-methyltransferase]]
[[Category: Histone-arginine N-methyltransferase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]

Revision as of 11:20, 20 October 2014

Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)

2oqb, resolution 1.69Å

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