Crystal structure and substrate-induced activation of ADAMTS13

The plasma metalloprotease ADAMTS13 regulates the platelet-tethering function of von Willebrand factor (VWF) in a shear-dependent manner. Here the authors present the ADAMTS13 crystal structure of the 70kDa N-terminal metalloprotease to spacer domains, and using kinetic measurements they identify a...

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Autores principales:	Anastasis Petri, Hyo Jung Kim, Yaoxian Xu, Rens de Groot, Chan Li, Aline Vandenbulcke, Karen Vanhoorelbeke, Jonas Emsley, James T. B. Crawley
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d27f55aa143e48378d1a3aee26caffd6
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spelling	oai:doaj.org-article:d27f55aa143e48378d1a3aee26caffd62021-12-02T15:35:05ZCrystal structure and substrate-induced activation of ADAMTS1310.1038/s41467-019-11474-52041-1723https://doaj.org/article/d27f55aa143e48378d1a3aee26caffd62019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11474-5https://doaj.org/toc/2041-1723The plasma metalloprotease ADAMTS13 regulates the platelet-tethering function of von Willebrand factor (VWF) in a shear-dependent manner. Here the authors present the ADAMTS13 crystal structure of the 70kDa N-terminal metalloprotease to spacer domains, and using kinetic measurements they identify a substrate binding induced allosteric mechanism for ADAMTS13, where VWF functions both as an activating cofactor and substrate.Anastasis PetriHyo Jung KimYaoxian XuRens de GrootChan LiAline VandenbulckeKaren VanhoorelbekeJonas EmsleyJames T. B. CrawleyNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Anastasis Petri Hyo Jung Kim Yaoxian Xu Rens de Groot Chan Li Aline Vandenbulcke Karen Vanhoorelbeke Jonas Emsley James T. B. Crawley Crystal structure and substrate-induced activation of ADAMTS13
description	The plasma metalloprotease ADAMTS13 regulates the platelet-tethering function of von Willebrand factor (VWF) in a shear-dependent manner. Here the authors present the ADAMTS13 crystal structure of the 70kDa N-terminal metalloprotease to spacer domains, and using kinetic measurements they identify a substrate binding induced allosteric mechanism for ADAMTS13, where VWF functions both as an activating cofactor and substrate.
format	article
author	Anastasis Petri Hyo Jung Kim Yaoxian Xu Rens de Groot Chan Li Aline Vandenbulcke Karen Vanhoorelbeke Jonas Emsley James T. B. Crawley
author_facet	Anastasis Petri Hyo Jung Kim Yaoxian Xu Rens de Groot Chan Li Aline Vandenbulcke Karen Vanhoorelbeke Jonas Emsley James T. B. Crawley
author_sort	Anastasis Petri
title	Crystal structure and substrate-induced activation of ADAMTS13
title_short	Crystal structure and substrate-induced activation of ADAMTS13
title_full	Crystal structure and substrate-induced activation of ADAMTS13
title_fullStr	Crystal structure and substrate-induced activation of ADAMTS13
title_full_unstemmed	Crystal structure and substrate-induced activation of ADAMTS13
title_sort	crystal structure and substrate-induced activation of adamts13
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/d27f55aa143e48378d1a3aee26caffd6
work_keys_str_mv	AT anastasispetri crystalstructureandsubstrateinducedactivationofadamts13 AT hyojungkim crystalstructureandsubstrateinducedactivationofadamts13 AT yaoxianxu crystalstructureandsubstrateinducedactivationofadamts13 AT rensdegroot crystalstructureandsubstrateinducedactivationofadamts13 AT chanli crystalstructureandsubstrateinducedactivationofadamts13 AT alinevandenbulcke crystalstructureandsubstrateinducedactivationofadamts13 AT karenvanhoorelbeke crystalstructureandsubstrateinducedactivationofadamts13 AT jonasemsley crystalstructureandsubstrateinducedactivationofadamts13 AT jamestbcrawley crystalstructureandsubstrateinducedactivationofadamts13
_version_	1718386686508924928

Crystal structure and substrate-induced activation of ADAMTS13

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