HDX-MS data on bRaf, bRaf/Cdc37 and bRaf/Cdc37/Hsp90 protein complexes
Ontology highlight
ABSTRACT:
INSTRUMENT(S): maXis II
ORGANISM(S): Homo Sapiens (ncbitaxon:9606)
SUBMITTER: 
Ioannis Gelis
PROVIDER: MSV000088635 | MassIVE | Tue Jan 04 07:44:00 GMT 2022
REPOSITORIES: MassIVE
Publications
Assembly mechanism of early Hsp90-Cdc37-kinase complexes.
Keramisanou Dimitra D Vasantha Kumar M V MV Boose Nicole N Abzalimov Rinat R RR Gelis Ioannis I
Science advances 20220316 11
Molecular chaperones have an essential role for the maintenance of a balanced protein homeostasis. Here, we investigate how protein kinases are recruited and loaded to the Hsp90-Cdc37 complex, the first step during Hsp90-mediated chaperoning that leads to enhanced client kinase stability and activation. We show that conformational dynamics of all partners is a critical feature of the underlying loading mechanism. The kinome co-chaperone Cdc37 exists primarily in a dynamic extended conformation b ...[more]
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