N-terminal domain (red), MD = middle domain (green), CTD = C-terminal domain (blue). Crystallographic structure of the ATP binding pocket of<unk>  where ATP is represented by a ball and stick figure (carbon atoms = grey, nitrogen = blue, oxygen = red, phosphorus = orange) and<unk>  is depicted as a solid surface (negatively charged = red, positively charged = blue, electrostatically neutral = grey). Pincer movement of<unk>  coupled to the ATPase cycle. NTD = N-terminal domain, MD = middle domain, CTD = C-terminal domain. The<unk>  chaperone cycle. X/Y represents an immature incompletely folded protein such a steroid receptor.<unk> ,<unk> , and p23 are partner chaperones while Hop is a co-chaperone. Also, X-X represents a mature properly folded protein dimer.<unk>  (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<unk>  inhibitors are investigated as anti-cancer drugs. Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species. 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. Heat shock protein 90<unk>  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.<unk>  is found in bacteria and all branches of eukarya, but it is apparently absent in archaea. Whereas cytoplasmic<unk>  is essential for viability under all conditions in eukaryotes, the bacterial homologue HtpG is dispensable under non-heat stress conditions. 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. However it was later discovered that<unk>  also has essential functions in unstressed cells.
Hsp90
HspE7
Bcl-xL
Bcl-2
Caspase-9
Mad2
IKK2
NLRP3