2oqb
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(New page: 200px<br /><applet load="2oqb" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oqb, resolution 1.690Å" /> '''Crystal structure o...)
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Revision as of 10:36, 23 January 2008
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Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)
Overview
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.
About this Structure
2OQB is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Histone-arginine N-methyltransferase, with EC number 2.1.1.125 Full crystallographic information is available from OCA.
Reference
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
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