Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms

The molecular basis of activin receptor-like kinase 1 (ALK1)-mediated endothelial bone morphogenetic protein (BMP) signalling is not fully understood. Here, the authors present crystal structures of the BMP10:ALK1 and prodomain-bound BMP9:ALK1 complexes, providing mechanistic insights into ALK1 sign...

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Autores principales:	Richard M. Salmon, Jingxu Guo, Jennifer H. Wood, Zhen Tong, John S. Beech, Aleksandra Lawera, Minmin Yu, David J. Grainger, Jill Reckless, Nicholas W. Morrell, Wei Li
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c95928c8f6c04cf69fb1889c1608aeab
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spelling	oai:doaj.org-article:c95928c8f6c04cf69fb1889c1608aeab2021-12-02T14:42:12ZMolecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms10.1038/s41467-020-15425-32041-1723https://doaj.org/article/c95928c8f6c04cf69fb1889c1608aeab2020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15425-3https://doaj.org/toc/2041-1723The molecular basis of activin receptor-like kinase 1 (ALK1)-mediated endothelial bone morphogenetic protein (BMP) signalling is not fully understood. Here, the authors present crystal structures of the BMP10:ALK1 and prodomain-bound BMP9:ALK1 complexes, providing mechanistic insights into ALK1 signalling specificity.Richard M. SalmonJingxu GuoJennifer H. WoodZhen TongJohn S. BeechAleksandra LaweraMinmin YuDavid J. GraingerJill RecklessNicholas W. MorrellWei LiNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Richard M. Salmon Jingxu Guo Jennifer H. Wood Zhen Tong John S. Beech Aleksandra Lawera Minmin Yu David J. Grainger Jill Reckless Nicholas W. Morrell Wei Li Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms
description	The molecular basis of activin receptor-like kinase 1 (ALK1)-mediated endothelial bone morphogenetic protein (BMP) signalling is not fully understood. Here, the authors present crystal structures of the BMP10:ALK1 and prodomain-bound BMP9:ALK1 complexes, providing mechanistic insights into ALK1 signalling specificity.
format	article
author	Richard M. Salmon Jingxu Guo Jennifer H. Wood Zhen Tong John S. Beech Aleksandra Lawera Minmin Yu David J. Grainger Jill Reckless Nicholas W. Morrell Wei Li
author_facet	Richard M. Salmon Jingxu Guo Jennifer H. Wood Zhen Tong John S. Beech Aleksandra Lawera Minmin Yu David J. Grainger Jill Reckless Nicholas W. Morrell Wei Li
author_sort	Richard M. Salmon
title	Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms
title_short	Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms
title_full	Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms
title_fullStr	Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms
title_full_unstemmed	Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms
title_sort	molecular basis of alk1-mediated signalling by bmp9/bmp10 and their prodomain-bound forms
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/c95928c8f6c04cf69fb1889c1608aeab
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Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms

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