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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