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Article

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

Nature communications - 16 Apr 2018

Rutz Daniel Andreas, Luo Qi, Freiburger Lee, Madl Tobias, Kaila Ville R I, Sattler Michael, Buchner Johannes

Abstract excerpt

Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established that conformational switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for switch points in the large middle-domain (Hsp90-M) is scarce. Here we report on a tryptophan residue in Hsp90-M as a new...

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Share to HSP90 Heat-Shock Proteins
Share to Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

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Identifiers

PMID: 29662162
DOI: 10.1038/s41467-018-03946-x
PMCID: PMC5902578

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