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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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| Publicado no: | Nat Commun |
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| Main Authors: | , , , , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Nature Publishing Group UK
2019
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| 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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