JMJD5 is a human arginyl C-3 hydroxylase

Jumonji-C domain containing protein 5 (JMJD5) is essential for animal development but its catalytic activity has remained elusive so far. Here the authors show that human JMJD5 is an arginyl-hydroxylase and present the cofactor, substrate and product bound JMJD5 crystal structures.

Enregistré dans:

Détails bibliographiques
Auteurs principaux:	Sarah E. Wilkins, Md. Saiful Islam, Joan M. Gannon, Suzana Markolovic, Richard J. Hopkinson, Wei Ge, Christopher J. Schofield, Rasheduzzaman Chowdhury
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2018
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/21f08a0de33a4534a7d964a1710edd68
Tags:	Ajouter un tag Pas de tags, Soyez le premier à ajouter un tag!

id	oai:doaj.org-article:21f08a0de33a4534a7d964a1710edd68
record_format	dspace
spelling	oai:doaj.org-article:21f08a0de33a4534a7d964a1710edd682021-12-02T17:32:03ZJMJD5 is a human arginyl C-3 hydroxylase10.1038/s41467-018-03410-w2041-1723https://doaj.org/article/21f08a0de33a4534a7d964a1710edd682018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03410-whttps://doaj.org/toc/2041-1723Jumonji-C domain containing protein 5 (JMJD5) is essential for animal development but its catalytic activity has remained elusive so far. Here the authors show that human JMJD5 is an arginyl-hydroxylase and present the cofactor, substrate and product bound JMJD5 crystal structures.Sarah E. WilkinsMd. Saiful IslamJoan M. GannonSuzana MarkolovicRichard J. HopkinsonWei GeChristopher J. SchofieldRasheduzzaman ChowdhuryNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sarah E. Wilkins Md. Saiful Islam Joan M. Gannon Suzana Markolovic Richard J. Hopkinson Wei Ge Christopher J. Schofield Rasheduzzaman Chowdhury JMJD5 is a human arginyl C-3 hydroxylase
description	Jumonji-C domain containing protein 5 (JMJD5) is essential for animal development but its catalytic activity has remained elusive so far. Here the authors show that human JMJD5 is an arginyl-hydroxylase and present the cofactor, substrate and product bound JMJD5 crystal structures.
format	article
author	Sarah E. Wilkins Md. Saiful Islam Joan M. Gannon Suzana Markolovic Richard J. Hopkinson Wei Ge Christopher J. Schofield Rasheduzzaman Chowdhury
author_facet	Sarah E. Wilkins Md. Saiful Islam Joan M. Gannon Suzana Markolovic Richard J. Hopkinson Wei Ge Christopher J. Schofield Rasheduzzaman Chowdhury
author_sort	Sarah E. Wilkins
title	JMJD5 is a human arginyl C-3 hydroxylase
title_short	JMJD5 is a human arginyl C-3 hydroxylase
title_full	JMJD5 is a human arginyl C-3 hydroxylase
title_fullStr	JMJD5 is a human arginyl C-3 hydroxylase
title_full_unstemmed	JMJD5 is a human arginyl C-3 hydroxylase
title_sort	jmjd5 is a human arginyl c-3 hydroxylase
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/21f08a0de33a4534a7d964a1710edd68
work_keys_str_mv	AT sarahewilkins jmjd5isahumanarginylc3hydroxylase AT mdsaifulislam jmjd5isahumanarginylc3hydroxylase AT joanmgannon jmjd5isahumanarginylc3hydroxylase AT suzanamarkolovic jmjd5isahumanarginylc3hydroxylase AT richardjhopkinson jmjd5isahumanarginylc3hydroxylase AT weige jmjd5isahumanarginylc3hydroxylase AT christopherjschofield jmjd5isahumanarginylc3hydroxylase AT rasheduzzamanchowdhury jmjd5isahumanarginylc3hydroxylase
_version_	1718380416045416448

JMJD5 is a human arginyl C-3 hydroxylase

Documents similaires