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3b3f
From Proteopedia
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| - | [[Image:3b3f.gif|left|200px]] | + | [[Image:3b3f.gif|left|200px]] |
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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''' | + | {{Structure |
| + | |PDB= 3b3f |SIZE=350|CAPTION= <scene name='initialview01'>3b3f</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''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== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3B3F is a [ | + | 3B3F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B3F OCA]. |
==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:// | + | 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] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:55:47 2008'' |
Revision as of 16:55, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Carm1, Prmt4 (Rattus norvegicus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 18:55:47 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
