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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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Detalhes bibliográficos
Publicado no:Nat Commun
Main Authors: 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: Artigo
Idioma:Inglês
Publicado em: Nature Publishing Group UK 2019
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC6327041/
https://ncbi.nlm.nih.gov/pubmed/30626866
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-018-07829-z
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