The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification

Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYST3/KAT6A. In addition to sa...

Descripción completa

Detalles Bibliográficos
Autores principales: Dreveny, Ingrid, Deeves, Sian E., Fulton, Joel, Yue, Baigong, Messmer, Marie, Bhattacharya, Amit, Collins, Hilary M., Heery, David M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Gene Regulation, Chromatin and Epigenetics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3902925/
https://www.ncbi.nlm.nih.gov/pubmed/24150941
http://dx.doi.org/10.1093/nar/gkt931

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3902925/
https://www.ncbi.nlm.nih.gov/pubmed/24150941
http://dx.doi.org/10.1093/nar/gkt931

Ejemplares similares