User:Yash Patankar/Sandbox 1
From Proteopedia
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{{STRUCTURE_3cin | PDB=3cin | SCENE= }} | {{STRUCTURE_3cin | PDB=3cin | SCENE= }} | ||
| - | Hsp90 is a ubiquitous molecular chaperone responsible for the governing of protein folding and regulation of many eukaryotic signaling pathways in the cell (Ali et al., 2006). It is involved in the activation of many regulatory and signaling client proteins under normal conditions in addition to the refolding of misfolding of a number of proteins during stress. | + | Hsp90, a 90 kDa heat-shock protein, is a ubiquitous molecular chaperone responsible for the governing of protein folding and regulation of many eukaryotic signaling pathways in the cell (Ali et al., 2006). It is a non-fibrous protein involved in the activation of many regulatory and signaling client proteins under normal conditions in addition to the refolding of misfolding of a number of proteins during stress (Ali et al., 2006; Pearl et al., 2008). Hsp90 is one of the most abundant proteins expressed in cells and it has been estimated to constitute upto 2% of the cellular proteins (Dollins et al., 2007). Hsp90 is found in all eukaryotes as well as bacteria with the exception of archae (Chen et al., 2006). Hsp90 has been shown to act as a buffer or capacitor of genetic variation in morphological evolution in Drosophila and other model organisms (Rutherford et al., 2007). Hsp90 is known to be required for the function of protein kinases such as ErbB2m Cdk4, B-Raf and Akt/protein kinase which are upregualted in cancerous cells (Pearl, 2005). |
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| + | The function of Hsp90 depends on its ability to hydrolyze ATP after it binds in the active site of the protein and hence, the inhibition of Hsp90 by ATP competitors or non-hydrolyzable ATP analogs leads to the promotion of client degradation. | ||
Revision as of 03:18, 7 December 2008
Hsp90
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| 3cin, resolution 1.70Å () | |||||||||
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| Ligands: | , , | ||||||||
| Gene: | TM1419, TM_1419 (Thermotoga maritima MSB8) | ||||||||
| Activity: | Inositol-3-phosphate synthase, with EC number 5.5.1.4 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Hsp90, a 90 kDa heat-shock protein, is a ubiquitous molecular chaperone responsible for the governing of protein folding and regulation of many eukaryotic signaling pathways in the cell (Ali et al., 2006). It is a non-fibrous protein involved in the activation of many regulatory and signaling client proteins under normal conditions in addition to the refolding of misfolding of a number of proteins during stress (Ali et al., 2006; Pearl et al., 2008). Hsp90 is one of the most abundant proteins expressed in cells and it has been estimated to constitute upto 2% of the cellular proteins (Dollins et al., 2007). Hsp90 is found in all eukaryotes as well as bacteria with the exception of archae (Chen et al., 2006). Hsp90 has been shown to act as a buffer or capacitor of genetic variation in morphological evolution in Drosophila and other model organisms (Rutherford et al., 2007). Hsp90 is known to be required for the function of protein kinases such as ErbB2m Cdk4, B-Raf and Akt/protein kinase which are upregualted in cancerous cells (Pearl, 2005).
The function of Hsp90 depends on its ability to hydrolyze ATP after it binds in the active site of the protein and hence, the inhibition of Hsp90 by ATP competitors or non-hydrolyzable ATP analogs leads to the promotion of client degradation.
