Molecular basis of the interaction of Hsp90 with its co-chaperone Hop.

ABSTRACT: The heat shock protein (Hsp) Hsp90 is one of the most abundant proteins in the cell. It controls the functional turnover of proteins being involved in protein folding, refolding, transport as well as protein degradation. Co-chaperones influence Hsp90's activity in different ways, among which the Hsp organizing protein (Hop) was found to inhibit its ATP hydrolysis upon binding. Despite the availability of a number of studies investigating the Hsp90:Hop complex, several aspects of the Hsp90:Hop interaction have remained unresolved. Here, we employed a combinatory approach comprising native polyacrylamide gel electrophoresis, isothermal titration calorimetry, multiangle light scattering, isothermal titration calorimetry, small-angle X-ray scattering, dynamic light scattering, and nuclear magn

SUBMITTER: Lott A 

PROVIDER: S-EPMC7679967 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature