Hsp90
Heat shock proteins with a molecular mass around 90kDa / From Wikipedia, the free encyclopedia
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Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase | |||||||||
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Identifiers | |||||||||
Symbol | HATPase_c | ||||||||
Pfam | PF02518 | ||||||||
Pfam clan | CL0025 | ||||||||
InterPro | IPR003594 | ||||||||
SMART | SM00387 | ||||||||
SCOP2 | 1ei1 / SCOPe / SUPFAM | ||||||||
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Hsp90 protein | |||||||||
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Identifiers | |||||||||
Symbol | Hsp90 | ||||||||
Pfam | PF00183 | ||||||||
InterPro | IPR020576 | ||||||||
PROSITE | PDOC00270 | ||||||||
SCOP2 | 1ah6 / SCOPe / SUPFAM | ||||||||
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Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species.[3] As their name implies, heat shock proteins protect cells when stressed by elevated temperatures. They account for 1–2% of total protein in unstressed cells. However, when cells are heated, the fraction of heat shock proteins increases to 4–6% of cellular proteins.[4]
Heat shock protein 90 (Hsp90) is one of the most common of the heat-related proteins. The "90" comes from the fact that it has a mass of roughly 90 kilodaltons. A 90 kDa protein is considered fairly large for a non-fibrous protein. Hsp90 is found in bacteria and all branches of eukarya, but it is apparently absent in archaea.[5] Whereas cytoplasmic Hsp90 is essential for viability under all conditions in eukaryotes, the bacterial homologue HtpG is dispensable under non-heat stress conditions.[6]
This protein was first isolated by extracting proteins from cells stressed by heating, dehydrating or by other means, all of which caused the cell's proteins to begin to denature.[7] However it was later discovered that Hsp90 also has essential functions in unstressed cells.