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QuickView for Heat shock protein Hsp90, conserved site (biogroup)
- Description:
- Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp). The 90 kDa heat shock protein, Hsp90, is one of the most abundant proteins in eukaryotic cells, comprising 1-2% of cellular proteins under non-stress conditions. Its contribution to various cellular processes including signal transduction, protein folding, protein degradation and morphological evolution has been extensively studied. The full functional activity of Hsp90 is gained in concert with other co-chaperones, playing an important role in the folding of newly synthesised proteins and stabilisation and refolding of denatured proteins after stress. Apart from its co-chaperones, Hsp90 binds to an array of client proteins, where the co-chaperone requirement varies and depends on the actual client. The sequences of hsp90s show a distinctive domain structure, with a highly-conserved N-terminal domain separated from a conserved, acidic C-terminal domain by a highly-acidic, flexible linker region.The signature pattern for the hsp90 family of proteins is located in a highly conserved region found in the N-terminal part of these proteins.
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