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Introduction
Molecular Mechanism of Hsp90 Machinery
Co-chaperones
TPR-Containing Co-Chaperones and Development of Hsp90 Inhibitors
Conclusion
100
The evolutionarily conserved molecular chaperone involved in the folding, stabilization, activation, and assembly of its client proteins.
What is Hsp 90?
100
The conformational changes of Hsp90's structure was recently determined using this method.
What is FRET (Fluorescence Resonance Energy Transfer)?
100
Co-Chaperones can modify Hsp90 activity in these two ways.
What are client protein recruitment and ATPase cycle regulation?
100
Development of Hsp90 inhibitors would have this benefit.
What is forced degradation of oncogenic client proteins?
100
Hsp90 chaperone machinery plays this central role in coordinating the dynamic networks of intra/intercellular proteins.
What acts as a molecular folding capacitor and hub for molecular assembly?
200
Also known as a substrate protein, Hsp90 binds these in the dimerization and middle domains.
What is a client protein?
200
The Hsp90 structure consists of these three domains.
What are the N-Terminal, Amphipathic loop, and C-terminal?
200
This co-factor arrests the ATPase cycle of Hsp90.
What is Cdc37?
200
This TPR-containing co-chaperone activates the Hsp90 ATPase cycle.
What is Aha1?
200
Hsp90 recognizes, stabilizes, and/or activates the wide range of structurally unrelated proteins in this manner.
What is unknown?
300
Name two Hsp90 client proteins.
What are kinases, transcription factors, and/or signaling molecules?
300
Hsp90 may exist as this many intermediates in the ATPase cycle.
What is 5?
300
Cdc37 does this.
Recruits kinase client proteins to Hsp90?
300
Current Hsp90 inhibitors block the ATPase cycle in this way.
What is docking to the N-terminal of the ATP binding pocket?
300
Hsp90 inhibitors could serve as potential therapeutic drugs to treat these diseases.
What are cancer, neurodegenerative, and inflammatory diseases?
400
How many Hsp90 proteins do prokaryotes and eukaryotes have?
Prokaryotes-1, eukaryotes- more than one.
400
The binding of ATP to the open Hsp90 dimer leads to the approximately 120 degree rotation of this segment.
What is the lid segment?
400
R and NLR proteins differ in this way.
What type of organism they are located in (plants, mammals)?
400
These are two TRP-containing co-chaperones.
What are HOP/Sti1 immunophilins (FKBP51, FKBP52, Cyp40), PP5/Ppt1 and CHIP?
400
These modifications to Hsp90 must still be researched before the protein is fully understood.
What are phosphorylation and acetylation?
500
The interaction between Hsp90 and its co-chaperones is useful in the development of these.
What are inhibitors for use as anti-cancer drugs?
500
This returns the Hsp90 to an open conformation with dissociated N-terminal domains and open lid segment.
What is ATP hydrolysis?
500
NLR and R proteins are both involved with this.
What are disease resistance and immunity?
500
The PPlase domain of FKBP52 is speculated to have this function.
What is adaptation for binding with motor proteins to allow intracellular movement along the microtubules?
500
This is required to develop disease specific drugs targeting Hsp90.
What is a detailed understanding of the chaperone machinery at both the systematic and atomic level?