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3mek
From Proteopedia
Contents |
Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine
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
3mek is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ 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
- ↑ 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
Categories: Histone-lysine N-methyltransferase | Homo sapiens | Arrowsmith, C H. | Bochkarev, A. | Bountra, C. | Dombrovski, L. | Edwards, A M. | Lam, R. | Li, Y. | Min, J. | SGC, Structural Genomics Consortium. | Weigelt, J. | Wu, H. | Chromatin modification | Chromatin regulator | Di-methylation | Dna-binding | Histone h3 | Histone methyltransferase | Metal-binding | Methyltransferase | Mynd-type zinc finger | Nucleus | S-adenosyl-l-methionine | Set and mynd domain-containing protein 3 | Set domain | Sgc | Structural genomic | Structural genomics consortium | Transcriptional activation | Transferase | Tri-methylation | Zinc finger mynd domain-containing protein 1 | Zinc-finger
