Heat shock 90kDa protein 1, alpha Adenovirus (Ad-HSP90)

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Also called molecular chaperones, heat shock proteins fall into six general families: HSP 90, HSP 70, HSP 60, the small molecular weight HSPs, the immunophilins and the HSP 110 family. The HSP 90 family consists of HSP 90 (alpha), HSP 90 (beta) and GRP 94, also called endoplasmin. The HSP 70 family includes HSP 70, HSC 70, GRP 78 and GRP 75. The low molecular weight family consists of HSP 10, HSP 27 (Heme Oxygenase 1), HSP 32 and HSP 40. The immunophilins include HSP 56 and bind immunosuppressant drugs. The HSP 110 family includes HSP 110, Apg-1 (also referred to as OSP 94), Apg-2 and HSP 105. HSP 47 binds specifically to collagen. Although the HSPs have long been known to bind ATP, the functional significance has not been established. Members of the HSP 70 family are implicated in acting as force generating motors, relying on the hydrolysis of ATP for their activity.