Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation

The DNA methyltransferase DNMT3A plays an important role in establishing the DNA methylation patterns during development and deregulation of DNMT3A is associated with hematological cancers, with the R882H mutation the most frequently occurring DNMT3A missense mutation in acute myeloid leukemia. Here...

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Autores principales:	Hiwot Anteneh, Jian Fang, Jikui Song
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/10c45f69c2c54eda9f4a5055aef152f6
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spelling	oai:doaj.org-article:10c45f69c2c54eda9f4a5055aef152f62021-12-02T17:31:25ZStructural basis for impairment of DNA methylation by the DNMT3A R882H mutation10.1038/s41467-020-16213-92041-1723https://doaj.org/article/10c45f69c2c54eda9f4a5055aef152f62020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16213-9https://doaj.org/toc/2041-1723The DNA methyltransferase DNMT3A plays an important role in establishing the DNA methylation patterns during development and deregulation of DNMT3A is associated with hematological cancers, with the R882H mutation the most frequently occurring DNMT3A missense mutation in acute myeloid leukemia. Here, the authors present the crystal structures of wild-type and R882H DNMT3A in complex with different DNA substrates and explain why the R882H mutation compromises the enzymatic activity of DNMT3A.Hiwot AntenehJian FangJikui SongNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hiwot Anteneh Jian Fang Jikui Song Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation
description	The DNA methyltransferase DNMT3A plays an important role in establishing the DNA methylation patterns during development and deregulation of DNMT3A is associated with hematological cancers, with the R882H mutation the most frequently occurring DNMT3A missense mutation in acute myeloid leukemia. Here, the authors present the crystal structures of wild-type and R882H DNMT3A in complex with different DNA substrates and explain why the R882H mutation compromises the enzymatic activity of DNMT3A.
format	article
author	Hiwot Anteneh Jian Fang Jikui Song
author_facet	Hiwot Anteneh Jian Fang Jikui Song
author_sort	Hiwot Anteneh
title	Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation
title_short	Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation
title_full	Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation
title_fullStr	Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation
title_full_unstemmed	Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation
title_sort	structural basis for impairment of dna methylation by the dnmt3a r882h mutation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/10c45f69c2c54eda9f4a5055aef152f6
work_keys_str_mv	AT hiwotanteneh structuralbasisforimpairmentofdnamethylationbythednmt3ar882hmutation AT jianfang structuralbasisforimpairmentofdnamethylationbythednmt3ar882hmutation AT jikuisong structuralbasisforimpairmentofdnamethylationbythednmt3ar882hmutation
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Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation

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