Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes

Ribosomes assemble through a process involving about 200 biogenesis factors and series of remodeling steps. Here the authors present the structures of the Rea1-MIDAS domain alone and in complex with its binding partners, shedding light on the process of mechanochemical release of the assembly factor...

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Autores principales:	Yasar Luqman Ahmed, Matthias Thoms, Valentin Mitterer, Irmgard Sinning, Ed Hurt
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/abf769c706a747f78941e47a6419e9d2
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spelling	oai:doaj.org-article:abf769c706a747f78941e47a6419e9d22021-12-02T17:02:03ZCrystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes10.1038/s41467-019-10922-62041-1723https://doaj.org/article/abf769c706a747f78941e47a6419e9d22019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10922-6https://doaj.org/toc/2041-1723Ribosomes assemble through a process involving about 200 biogenesis factors and series of remodeling steps. Here the authors present the structures of the Rea1-MIDAS domain alone and in complex with its binding partners, shedding light on the process of mechanochemical release of the assembly factors Rsa4 and Ytm1 from the pre-60S particle.Yasar Luqman AhmedMatthias ThomsValentin MittererIrmgard SinningEd HurtNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yasar Luqman Ahmed Matthias Thoms Valentin Mitterer Irmgard Sinning Ed Hurt Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes
description	Ribosomes assemble through a process involving about 200 biogenesis factors and series of remodeling steps. Here the authors present the structures of the Rea1-MIDAS domain alone and in complex with its binding partners, shedding light on the process of mechanochemical release of the assembly factors Rsa4 and Ytm1 from the pre-60S particle.
format	article
author	Yasar Luqman Ahmed Matthias Thoms Valentin Mitterer Irmgard Sinning Ed Hurt
author_facet	Yasar Luqman Ahmed Matthias Thoms Valentin Mitterer Irmgard Sinning Ed Hurt
author_sort	Yasar Luqman Ahmed
title	Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes
title_short	Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes
title_full	Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes
title_fullStr	Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes
title_full_unstemmed	Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes
title_sort	crystal structures of rea1-midas bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/abf769c706a747f78941e47a6419e9d2
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Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes

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