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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''' | '''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''' | ||
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[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Troffer-Charlier, N.]] | [[Category: Troffer-Charlier, N.]] | ||
[[Category: | [[Category: Alternative splicing]] | ||
[[Category: | [[Category: Catalytic domain]] | ||
[[Category: | [[Category: Chromatin regulator]] | ||
[[Category: | [[Category: Cytoplasm]] | ||
[[Category: | [[Category: Mrna processing]] | ||
[[Category: | [[Category: Mrna splicing]] | ||
[[Category: | [[Category: Nucleus]] | ||
[[Category: | [[Category: Protein arginine methyltransferase]] | ||
[[Category: | [[Category: S-adenosyl-l-methionine]] | ||
[[Category: | [[Category: Transcription]] | ||
[[Category: | [[Category: Transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:21:29 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:21, 4 May 2008
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. 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 20:21:29 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Rattus norvegicus
- Single protein
- Cavarelli, J.
- Cura, V.
- Hassenboehler, P.
- Moras, D.
- Troffer-Charlier, N.
- Alternative splicing
- Catalytic domain
- Chromatin regulator
- Cytoplasm
- Mrna processing
- Mrna splicing
- Nucleus
- Protein arginine methyltransferase
- S-adenosyl-l-methionine
- Transcription
- Transcription regulation
