Sandbox Reserved 1472
From Proteopedia
| Line 9: | Line 9: | ||
== 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> | + | 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 co-chaperone for Hsp90. |
| - | . | + | |
== Disease == | == Disease == | ||
Revision as of 18:21, 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. |
To get started:
More help: Help:Editing |
This page is reserved for Tim
Contents |
Hsp90-Cdc37-Cdk4 Complex
|
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.
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 co-chaperone for Hsp90.
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. </StructureSection>
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
