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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
The SET- and MYND-domain containing (Smyd) proteins constitute a special subfamily of the SET-containing lysine methyltransferases. Here we present the structure of full-length human Smyd3 in complex with S-adenosyl-l-homocysteine at 2.8 Å resolution. Smyd3 affords the first example that other regio...
| Autores principales: | , , , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Oxford University Press
2011
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3105404/ https://www.ncbi.nlm.nih.gov/pubmed/21266482 http://dx.doi.org/10.1093/nar/gkr019 |