Interaction of hsp 90 with p53 and Its mutated form and their comparison

Abstract

The binding of one signaling protein to another serve to recruit a signaling protein to a locat ion where it is activated and where it is needed to carry out its function, it induce conformational changes that affect activity or accessibility of additional binding domains, permitting additional protein interactions. If in a cell interaction disappearance will make cell deaf and blind, paralytic and finally will disintegrate.Hsp90 are molecular chaperones involved in stress response and
normal biosynthetic and homeostatic control mechanisms of the cell .It interact with different clients such as protein (kinases, transcription factor, and structurally unrelated protein), activate and direct it to proteasomal degradation. Disrupting the interaction between Hsp 90 and its client protein controls its biogenesis, stability and activity. The question arises is how the Hsp 90 recognizes p53 protein and what region of Hsp 90 are interacting with it. In this study the basis
of interaction of Hsp 90 with p53 is predicted by identifying unveiled hydrophobicity patches,location of binding site ,charge distribution and docking. Hydrophobic patches with hydropathy index similarity between Hsp 90 and p53 is predicted.The charge distribution and overall hydrophobicity was also compared . Protein –protein docking is studied using HEX which predicts that human Hsp 90 and wild type p53 form stable complex ,this is compared with mutant type p53.