Cargando…
Structural Chemistry of Human SET Domain Protein Methyltransferases
There are about fifty SET domain protein methyltransferases (PMTs) in the human genome, that transfer a methyl group from S-adenosyl-L-methionine (SAM) to substrate lysines on histone tails or other peptides. A number of structures in complex with cofactor, substrate, or inhibitors revealed the mech...
Autor principal: | Schapira, Matthieu |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Bentham Open
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3178901/ https://www.ncbi.nlm.nih.gov/pubmed/21966348 http://dx.doi.org/10.2174/1875397301005010085 |
Ejemplares similares
-
Structural biology and chemistry of protein arginine methyltransferases
por: Schapira, Matthieu, et al.
Publicado: (2014) -
The SET-domain protein superfamily: protein lysine methyltransferases
por: Dillon, Shane C, et al.
Publicado: (2005) -
Structural Biology of Human H3K9 Methyltransferases
por: Wu, Hong, et al.
Publicado: (2010) -
Methyltransferase Inhibitors: Competing with, or Exploiting the Bound Cofactor
por: Ferreira de Freitas, Renato, et al.
Publicado: (2019) -
Trimethylation of Histone H3 Lysine 36 by Human Methyltransferase PRDM9 Protein
por: Eram, Mohammad S., et al.
Publicado: (2014)