Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization

Bone morphogenetic protein (BMP) receptors are single pass transmembrane serine/threonine kinases that form tetrameric complexes comprised of two type I and two type II BMP receptors. Here the authors characterize a structure of an active type I/type II kinase tetramer providing insight into molecul...

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Autores principales:	Christopher Agnew, Pelin Ayaz, Risa Kashima, Hanna S. Loving, Prajakta Ghatpande, Jennifer E. Kung, Eric S. Underbakke, Yibing Shan, David E. Shaw, Akiko Hata, Natalia Jura
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2da61e530b6043e1b871d8b220f4580b
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spelling	oai:doaj.org-article:2da61e530b6043e1b871d8b220f4580b2021-12-02T15:10:35ZStructural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization10.1038/s41467-021-25248-52041-1723https://doaj.org/article/2da61e530b6043e1b871d8b220f4580b2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25248-5https://doaj.org/toc/2041-1723Bone morphogenetic protein (BMP) receptors are single pass transmembrane serine/threonine kinases that form tetrameric complexes comprised of two type I and two type II BMP receptors. Here the authors characterize a structure of an active type I/type II kinase tetramer providing insight into molecular mechanism driving ligand-induced signaling.Christopher AgnewPelin AyazRisa KashimaHanna S. LovingPrajakta GhatpandeJennifer E. KungEric S. UnderbakkeYibing ShanDavid E. ShawAkiko HataNatalia JuraNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Christopher Agnew Pelin Ayaz Risa Kashima Hanna S. Loving Prajakta Ghatpande Jennifer E. Kung Eric S. Underbakke Yibing Shan David E. Shaw Akiko Hata Natalia Jura Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization
description	Bone morphogenetic protein (BMP) receptors are single pass transmembrane serine/threonine kinases that form tetrameric complexes comprised of two type I and two type II BMP receptors. Here the authors characterize a structure of an active type I/type II kinase tetramer providing insight into molecular mechanism driving ligand-induced signaling.
format	article
author	Christopher Agnew Pelin Ayaz Risa Kashima Hanna S. Loving Prajakta Ghatpande Jennifer E. Kung Eric S. Underbakke Yibing Shan David E. Shaw Akiko Hata Natalia Jura
author_facet	Christopher Agnew Pelin Ayaz Risa Kashima Hanna S. Loving Prajakta Ghatpande Jennifer E. Kung Eric S. Underbakke Yibing Shan David E. Shaw Akiko Hata Natalia Jura
author_sort	Christopher Agnew
title	Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization
title_short	Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization
title_full	Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization
title_fullStr	Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization
title_full_unstemmed	Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization
title_sort	structural basis for alk2/bmpr2 receptor complex signaling through kinase domain oligomerization
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2da61e530b6043e1b871d8b220f4580b
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Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization

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