Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition

The human enzyme MTHFR links the folate and methionine cycles, which are essential for the biosynthesis of nucleotides and proteins. Here, the authors present the crystal structure and biochemical analysis of human MTHFR, providing molecular insights into its function and regulation in higher eukary...

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Autores principales:	D. Sean Froese, Jolanta Kopec, Elzbieta Rembeza, Gustavo Arruda Bezerra, Anselm Erich Oberholzer, Terttu Suormala, Seraina Lutz, Rod Chalk, Oktawia Borkowska, Matthias R. Baumgartner, Wyatt W. Yue
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/81b79808dd01406c825d1806af1a047c
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spelling	oai:doaj.org-article:81b79808dd01406c825d1806af1a047c2021-12-02T15:34:42ZStructural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition10.1038/s41467-018-04735-22041-1723https://doaj.org/article/81b79808dd01406c825d1806af1a047c2018-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04735-2https://doaj.org/toc/2041-1723The human enzyme MTHFR links the folate and methionine cycles, which are essential for the biosynthesis of nucleotides and proteins. Here, the authors present the crystal structure and biochemical analysis of human MTHFR, providing molecular insights into its function and regulation in higher eukaryotes.D. Sean FroeseJolanta KopecElzbieta RembezaGustavo Arruda BezerraAnselm Erich OberholzerTerttu SuormalaSeraina LutzRod ChalkOktawia BorkowskaMatthias R. BaumgartnerWyatt W. YueNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q D. Sean Froese Jolanta Kopec Elzbieta Rembeza Gustavo Arruda Bezerra Anselm Erich Oberholzer Terttu Suormala Seraina Lutz Rod Chalk Oktawia Borkowska Matthias R. Baumgartner Wyatt W. Yue Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition
description	The human enzyme MTHFR links the folate and methionine cycles, which are essential for the biosynthesis of nucleotides and proteins. Here, the authors present the crystal structure and biochemical analysis of human MTHFR, providing molecular insights into its function and regulation in higher eukaryotes.
format	article
author	D. Sean Froese Jolanta Kopec Elzbieta Rembeza Gustavo Arruda Bezerra Anselm Erich Oberholzer Terttu Suormala Seraina Lutz Rod Chalk Oktawia Borkowska Matthias R. Baumgartner Wyatt W. Yue
author_facet	D. Sean Froese Jolanta Kopec Elzbieta Rembeza Gustavo Arruda Bezerra Anselm Erich Oberholzer Terttu Suormala Seraina Lutz Rod Chalk Oktawia Borkowska Matthias R. Baumgartner Wyatt W. Yue
author_sort	D. Sean Froese
title	Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition
title_short	Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition
title_full	Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition
title_fullStr	Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition
title_full_unstemmed	Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition
title_sort	structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and s-adenosylmethionine inhibition
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/81b79808dd01406c825d1806af1a047c
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Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition

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