3b3f
From Proteopedia
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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
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
3B3F is a Single protein structure of sequence from Rattus norvegicus with as ligand. 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
Page seeded by OCA on Wed Jan 23 12:30:02 2008
Categories: Rattus norvegicus | Single protein | Cavarelli, J. | Cura, V. | Hassenboehler, P. | Moras, D. | Troffer-Charlier, N. | SAH | Alternative splicing | Catalytic domain | Chromatin regulator | Cytoplasm | Mrna processing | Mrna splicing | Nucleus | Protein arginine methyltransferase | S-adenosyl-l-methionine | Transcription | Transcription regulation
