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2v74
From Proteopedia
(New page: 200px<br /> <applet load="2v74" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v74, resolution 2.70Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2V74 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with SAH as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2V74 OCA]]. | + | 2V74 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with SAH as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Histone-arginine_N-methyltransferase Histone-arginine N-methyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2V74 OCA]]. |
==Reference== | ==Reference== | ||
Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase., Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH, EMBO J. 2007 Sep 20;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17882261 17882261] | Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase., Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH, EMBO J. 2007 Sep 20;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17882261 17882261] | ||
| + | [[Category: Histone-arginine N-methyltransferase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:53:09 2007'' |
Revision as of 15:48, 30 October 2007
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CRYSTAL STRUCTURE OF COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1), IN COMPLEX WITH S-ADENOSYL-HOMOCYSTEINE
Overview
Coactivator-associated arginine methyltransferase (CARM1) is a, transcriptional coactivator that methylates Arg17 and Arg26 in histone H3., CARM1 contains a conserved protein arginine methyltransferase (PRMT), catalytic core flanked by unique pre- and post-core regions. The crystal, structures of the CARM1 catalytic core in the apo and holo states reveal, cofactor-dependent formation of a substrate-binding groove providing a, specific access channel for arginine to the active site. The groove is, supported by the first eight residues of the post-core region, (C-extension), not present in other PRMTs. In vitro methylation assays, show that the C-extension is essential for all histone H3 methylation, activity, whereas the pre-core region is required for methylation of, Arg26, but not Arg17. ... [(full description)]
About this Structure
2V74 is a [Single protein] structure of sequence from [Mus musculus] with SAH as [ligand]. Active as [Histone-arginine N-methyltransferase], with EC number [2.1.1.125]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase., Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH, EMBO J. 2007 Sep 20;. PMID:17882261
Page seeded by OCA on Tue Oct 30 17:53:09 2007
Categories: Histone-arginine N-methyltransferase | Mus musculus | Single protein | Hassler, M. | Pearl, L.H. | Roe, S.M. | Thompson-Vale, V. | Yue, W.W. | SAH | Alternative splicing | Arginine methyltransferase | Chromatin regulator | Co- activator | Cytoplasm | Histone modification | Methyltransferase | Nucleus | S-adenosyl-l-methionine | Transcription | Transcription regulation | Transferase
