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...

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Detalles Bibliográficos
Autores principales: Xu, Shutong, Wu, Jian, Sun, Bingfa, Zhong, Chen, Ding, Jianping
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
Structural Biology
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

Internet

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

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