3oxg

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[[Image:3oxg.png|left|200px]]
 
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{{STRUCTURE_3oxg| PDB=3oxg | SCENE= }}
{{STRUCTURE_3oxg| PDB=3oxg | SCENE= }}
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===human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III)===
===human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III)===
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{{ABSTRACT_PUBMED_21266482}}
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==Function==
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[[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>
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{{ABSTRACT_PUBMED_21266482}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:021266482</ref><references group="xtra"/>
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<ref group="xtra">PMID:021266482</ref><references group="xtra"/><references/>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 07:54, 16 May 2013

Template:STRUCTURE 3oxg

Contents

human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III)

Template:ABSTRACT PUBMED 21266482

Function

[SMYD3_HUMAN] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.[1] [2]

About this Structure

3oxg is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Xu S, Wu J, Sun B, Zhong C, Ding J. Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding. Nucleic Acids Res. 2011 Jan 25. PMID:21266482 doi:10.1093/nar/gkr019
  1. ↑ Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat Cell Biol. 2004 Aug;6(8):731-40. Epub 2004 Jul 4. PMID:15235609 doi:10.1038/ncb1151
  2. ↑ Van Aller GS, Reynoird N, Barbash O, Huddleston M, Liu S, Zmoos AF, McDevitt P, Sinnamon R, Le B, Mas G, Annan R, Sage J, Garcia BA, Tummino PJ, Gozani O, Kruger RG. Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5 methylation. Epigenetics. 2012 Apr;7(4):340-3. doi: 10.4161/epi.19506. Epub 2012 Apr 1. PMID:22419068 doi:10.4161/epi.19506

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