3b3f: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2oqb|2OQB]], [[3b3g|3B3G]], [[3b3j|3B3J]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b3f OCA], [http://www.ebi.ac.uk/pdbsum/3b3f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b3f RCSB]</span> | |||
}} | }} | ||
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[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Troffer-Charlier, N.]] | [[Category: Troffer-Charlier, N.]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: catalytic domain]] | [[Category: catalytic domain]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:22:42 2008'' | ||
Revision as of 05:22, 31 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Carm1, Prmt4 (Rattus norvegicus) | ||||||
| Related: | 2OQB, 3B3G, 3B3J
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
OverviewOverview
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 StructureAbout this Structure
3B3F is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- 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