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>. 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>. Cdk4 | + | 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>. Cdk4 is a part of a kinase complex that is needed for cell cycle G1 phase progression. For the activation of Cdk4 there must be proper folding, binding of the regulator cyclin D, ATP binding, a positioning of the active site near the ATP binding site and phosphorylation of the amino acid residue T172. Hsp90 and the co-chaperone Cdc37 plays a crucial role in the late folding process of Cdk4 needed for its activation of which is critical for cell development<ref>PMID:29782836<ref/>. |
| + | |||
== Disease == | == Disease == | ||
Revision as of 20:06, 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
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 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]. Cdk4 is a part of a kinase complex that is needed for cell cycle G1 phase progression. For the activation of Cdk4 there must be proper folding, binding of the regulator cyclin D, ATP binding, a positioning of the active site near the ATP binding site and phosphorylation of the amino acid residue T172. Hsp90 and the co-chaperone Cdc37 plays a crucial role in the late folding process of Cdk4 needed for its activation of which is critical for cell development[3]
