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3b3f

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{{STRUCTURE_3b3f| PDB=3b3f | SCENE= }}
{{STRUCTURE_3b3f| PDB=3b3f | SCENE= }}
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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'''
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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===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17882262 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17882262}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/17882262 17882262]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17882262 17882262]
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Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1., Troffer-Charlier N, Cura V, Hassenboehler P, Moras D, Cavarelli J, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):330-3. Epub 2007 Mar 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17401209 17401209]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:21:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:59:01 2008''

Revision as of 12:59, 29 July 2008

Image:3b3f.png

Template:STRUCTURE 3b3f

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

Template:ABSTRACT PUBMED 17882262

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

Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1., Troffer-Charlier N, Cura V, Hassenboehler P, Moras D, Cavarelli J, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):330-3. Epub 2007 Mar 30. PMID:17401209

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