NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90

The hsp90 chaperones govern the function of essential client proteins critical for normal cell function as well as cancer initiation and progression. Hsp90 activity is driven by ATP, which binds to the N-terminal domain and induces large conformational changes that are required for client maturation...

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Bibliographic Details
Published in:J Biol Chem
Main Authors: Huck, John D., Que, Nanette L. S., Immormino, Robert M., Shrestha, Liza, Taldone, Tony, Chiosis, Gabriela, Gewirth, Daniel T.
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2019
Subjects:
Protein Structure and Folding
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC6827299/
https://ncbi.nlm.nih.gov/pubmed/31501246
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.009960
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