This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Hsp90 molecular chaperones are responsible for the conformational maturation of linear peptides into active three-dimensional enzymes and receptors. Examples of proteins dependent on the Hsp90 protein folding machinery include steroid hormone receptors, Src kinase, Her-2 kinase, Raf, p185, mutant p53, telomerase, PKR, telomerase, nitric oxide synthase, CDK-4 and CDK-6 to name a few. As Hsp90 continues to evolve into a popular target for the treatment of cancer more information is required to validate its role in the maturation of key regulatory proteins. For example, it is not known how many client proteins require Hsp90 for folding, or which of the four known forms of Hsp90 (a, b, GRP94, or TRP), immunophilin (FKBP51, FKBP52, or Cyp40), or cochaperone participate in the folding of various individual client proteins.
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