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''' | '''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
Categories: 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
