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== Function == | == Function == | ||
| - | The Hsp90-Cdc37-Cdk4 complex is made up of the Heat Shock Protein 90 chaperone molecule, Cell Division Cycle 37 co-chaperone molecule, and the Cyclin-dependent 4 Kinase client molecule. Hsp90 is a 90-kDa protein that acts as a molecular chaperone for a variety of client proteins the majority of which are involved in signal transduction. It belongs to a group of proteins called heat shock proteins. Heat shock proteins are named for the response that organisms exhibit due to stresses at a cellular level such as elevated temperatures beyond the normal existing environment cells usually cope with. A major feature of this response is an alteration of an organism’s gene expression through increased heat shock protein production<ref>PMID:30158430</ref>. Cdc37 is one the the main co-chaperones of Hsp90. It is classified as a client recruiter of kinase proteins for Hsp90. | + | The Hsp90-Cdc37-Cdk4 complex is made up of the Heat Shock Protein 90 chaperone molecule, Cell Division Cycle 37 co-chaperone molecule, and the Cyclin-dependent 4 Kinase client molecule. Hsp90 is a 90-kDa protein that acts as a molecular chaperone for a variety of client proteins the majority of which are involved in signal transduction. It belongs to a group of proteins called heat shock proteins. Heat shock proteins are named for the response that organisms exhibit due to stresses at a cellular level such as elevated temperatures beyond the normal existing environment cells usually cope with. A major feature of this response is an alteration of an organism’s gene expression through increased heat shock protein production<ref>PMID:30158430</ref>. Cdc37 is one the the main co-chaperones of Hsp90. It is classified as a client recruiter of kinase proteins for Hsp90. There is evidence Cdc37 works by recognizing conformational instability of kinase clients and changing their folding landscapes as it binds to the client and recruits it to Hsp90<ref>PMID:29267381</ref>. |
== Disease == | == Disease == | ||
Revision as of 19:30, 4 December 2018
| This Sandbox is Reserved from November 5 2018 through January 1, 2019 for use in the course "CHEM 4923: Senior Project taught by Christina R. Bourne at the University of Oklahoma, Norman, USA. This reservation includes Sandbox Reserved 1471 through Sandbox Reserved 1478. |
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Hsp90-Cdc37-Cdk4 Complex
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Function
The Hsp90-Cdc37-Cdk4 complex is made up of the Heat Shock Protein 90 chaperone molecule, Cell Division Cycle 37 co-chaperone molecule, and the Cyclin-dependent 4 Kinase client molecule. Hsp90 is a 90-kDa protein that acts as a molecular chaperone for a variety of client proteins the majority of which are involved in signal transduction. It belongs to a group of proteins called heat shock proteins. Heat shock proteins are named for the response that organisms exhibit due to stresses at a cellular level such as elevated temperatures beyond the normal existing environment cells usually cope with. A major feature of this response is an alteration of an organism’s gene expression through increased heat shock protein production[1]. Cdc37 is one the the main co-chaperones of Hsp90. It is classified as a client recruiter of kinase proteins for Hsp90. There is evidence Cdc37 works by recognizing conformational instability of kinase clients and changing their folding landscapes as it binds to the client and recruits it to Hsp90[2].
Disease
Relevance
Structural highlights
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References
- ↑ Hoter A, El-Sabban ME, Naim HY. The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease. Int J Mol Sci. 2018 Aug 29;19(9). pii: ijms19092560. doi: 10.3390/ijms19092560. PMID:30158430 doi:http://dx.doi.org/10.3390/ijms19092560
- ↑ Czemeres J, Buse K, Verkhivker GM. Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains. PLoS One. 2017 Dec 21;12(12):e0190267. doi: 10.1371/journal.pone.0190267., eCollection 2017. PMID:29267381 doi:http://dx.doi.org/10.1371/journal.pone.0190267
