A switch point in the molecular chaperone Hsp90 responding to client interaction

The heat shock protein 90 (Hsp90) chaperone undergoes large conformational changes during its functional cycle. Here the authors combine in vivo, biochemical, biophysical and computational approaches and provide insights into the allosteric regulation of Hsp90 by identifying and characterizing a swi...

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Autores principales: Daniel Andreas Rutz, Qi Luo, Lee Freiburger, Tobias Madl, Ville R. I. Kaila, Michael Sattler, Johannes Buchner
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/eb99df2bef0c4d18881cbe90d73b5d15
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spelling oai:doaj.org-article:eb99df2bef0c4d18881cbe90d73b5d152021-12-02T14:40:10ZA switch point in the molecular chaperone Hsp90 responding to client interaction10.1038/s41467-018-03946-x2041-1723https://doaj.org/article/eb99df2bef0c4d18881cbe90d73b5d152018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03946-xhttps://doaj.org/toc/2041-1723The heat shock protein 90 (Hsp90) chaperone undergoes large conformational changes during its functional cycle. Here the authors combine in vivo, biochemical, biophysical and computational approaches and provide insights into the allosteric regulation of Hsp90 by identifying and characterizing a switch point in the Hsp90 middle domain.Daniel Andreas RutzQi LuoLee FreiburgerTobias MadlVille R. I. KailaMichael SattlerJohannes BuchnerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Daniel Andreas Rutz
Qi Luo
Lee Freiburger
Tobias Madl
Ville R. I. Kaila
Michael Sattler
Johannes Buchner
A switch point in the molecular chaperone Hsp90 responding to client interaction
description The heat shock protein 90 (Hsp90) chaperone undergoes large conformational changes during its functional cycle. Here the authors combine in vivo, biochemical, biophysical and computational approaches and provide insights into the allosteric regulation of Hsp90 by identifying and characterizing a switch point in the Hsp90 middle domain.
format article
author Daniel Andreas Rutz
Qi Luo
Lee Freiburger
Tobias Madl
Ville R. I. Kaila
Michael Sattler
Johannes Buchner
author_facet Daniel Andreas Rutz
Qi Luo
Lee Freiburger
Tobias Madl
Ville R. I. Kaila
Michael Sattler
Johannes Buchner
author_sort Daniel Andreas Rutz
title A switch point in the molecular chaperone Hsp90 responding to client interaction
title_short A switch point in the molecular chaperone Hsp90 responding to client interaction
title_full A switch point in the molecular chaperone Hsp90 responding to client interaction
title_fullStr A switch point in the molecular chaperone Hsp90 responding to client interaction
title_full_unstemmed A switch point in the molecular chaperone Hsp90 responding to client interaction
title_sort switch point in the molecular chaperone hsp90 responding to client interaction
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/eb99df2bef0c4d18881cbe90d73b5d15
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