Ontology highlight
ABSTRACT:
SUBMITTER: Oroz J
PROVIDER: S-EPMC6699087 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Oroz Javier J Blair Laura J LJ Zweckstetter Markus M
Protein science : a publication of the Protein Society 20190806 9
Hsp90 is an essential chaperone that requires large allosteric changes to determine its ATPase activity and client binding. The co-chaperone Aha1, which is the major ATPase stimulator in eukaryotes, is important for regulation of Hsp90's allosteric timing. Little is known, however, about the structure of the Hsp90/Aha1 complex. Here, we characterize the solution structure of unmodified human Hsp90/Aha1 complex using NMR spectroscopy. We show that the 214-kDa complex forms by a two-step binding m ...[more]