Biopolym. Cell. 2009; 25(5):372-383.
Hsp90 molecular chaperone: structure, functions and participation in the cardio-vascular pathologies
1Kroupskaya I. V.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680


This review is devoted to analysis of structural and functional properties of molecular chaperon Hsp90. Hsp90 are highly widespread family of heat shock proteins . Protein is found in eubacteria and all branches of eukarya, but it is apparently absent in archaea. It is one of key regulators of numerous signalling pathways, cell growth and development, apoptosis, induction of autoimmunity and progression of heart failure. The full functional activity of Hsp90 shows up in a complex with other molecular chaperones and co-chaperones. Molecular interactions between chaperones, different signaling proteins and protein-partners are highly crucial for the normal functioning of signaling pathways and its destruction are causes the alteration of cell physiology up to its death.
Keywords: Hsp90, domain, structure, signaling pathways, apoptosis


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