Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling

Histone demethylase KDM5A removes methyl marks from lysine 4 of histone H3 and is often overexpressed in cancer. The in vitro demethylase activity of KDM5A is allosterically enhanced by binding of its product, unmodified H3 peptides, to its PHD1 reader domain. However, the molecular basis of this al...

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Detalles Bibliográficos
Autores principales: Longbotham, James E., Chio, Cynthia M., Dharmarajan, Venkatasubramanian, Trnka, Michael J., Torres, Idelisse Ortiz, Goswami, Devrishi, Ruiz, Karen, Burlingame, Alma L., Griffin, Patrick R., Fujimori, Danica Galonić
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6327041/
https://www.ncbi.nlm.nih.gov/pubmed/30626866
http://dx.doi.org/10.1038/s41467-018-07829-z

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6327041/
https://www.ncbi.nlm.nih.gov/pubmed/30626866
http://dx.doi.org/10.1038/s41467-018-07829-z

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