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HDX-MS data on bRaf, bRaf/Cdc37 and bRaf/Cdc37/Hsp90 protein complexes

ABSTRACT: HDX-MS data on bRaf, bRaf/Cdc37 and bRaf/Cdc37/Hsp90 protein complexes

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

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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]

PMID: 35294247

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