Biopolymers and cell. 2009; 25 (5): 372 - 383

Hsp90 molecular chaperone: structure, functions and participation in cardio-vascular pathologies

I. V. Kroupskaya

Institute of molecular biology and genetics NAS of Ukraine

150, Zabolotnogo Str, Kyiv Ukraine, 03680

The review is devoted to the analysis of structural and functional properties of molecular chaperon Hsp90. Hsp90 is a representative of highly widespread family of heat shock proteins. The 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 signalling proteins and protein-partners are highly crucial for the normal functioning of signalling pathways and their destruction causes an alteration in the cell physiology up to its death.

Keywords: Hsp90, domain, cristal structure, signalling pathways, apoptosis.