Peptide corresponding to the sequence EEVHHGEEEVEC within N-terminal part of human Hsp90.
Hsp90 (heat shock protein 90) is one of the most abundant chaperones in the cytosol of eukaryotic cells. It interacts with various proteins, including protein kinases and transcription factors, and either facilitates their stabilization and activation or directs them for proteasomal degradation. Hsp90 thus affects multiple signaling pathways and biological processes and modulation of this single target offers the prospect of simultaneous intervence to various key points of oncogenic transformation. Hsp90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis. There are two isoforms, alpha and beta, of vertebrate Hsp90. Whereas Hsp90 beta is expressed constitutively to a high level, Hsp90 alpha is stress-inducible and is overexpressed in many cancerous cells.
