2oqb
From Proteopedia
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[[Image:2oqb.gif|left|200px]] | [[Image:2oqb.gif|left|200px]] | ||
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'''Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)''' | '''Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cavarelli, J.]] | [[Category: Cavarelli, J.]] | ||
- | [[Category: | + | [[Category: Activation domain]] |
- | [[Category: | + | [[Category: Protein arginine methyltransferase]] |
- | [[Category: | + | [[Category: Transcriptional regulation]] |
- | [[Category: | + | [[Category: Transferase,gene regulation]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:26:45 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 08:26, 4 May 2008
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. 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 Sun May 4 11:26:45 2008