Molecular mechanism for USP7-mediated DNMT1 stabilization by acetylation
Molecular mechanism for USP7-mediated DNMT1 stabilization by acetylation
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Author / Creator
Cheng, Jingdong , Yang, Huirong , Fang, Jian , Ma, Lixiang , Gong, Rui , Wang, Ping , Li, Ze and Xu, Yanhui
Publisher
London: Nature Publishing Group UK
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Language
English
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Publisher
London: Nature Publishing Group UK
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Contents
DNMT1 is an important epigenetic regulator that plays a key role in the maintenance of DNA methylation. Here we determined the crystal structure of DNMT1 in complex with USP7 at 2.9 Å resolution. The interaction between the two proteins is primarily mediated by an acidic pocket in USP7 and Lysine residues within DNMT1’s KG linker. This intermolecul...
Alternative Titles
Full title
Molecular mechanism for USP7-mediated DNMT1 stabilization by acetylation
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4432644
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4432644
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/ncomms8023
