Identification of the Factors Responsible for the Interaction of Hsp90α and its Client Proteins
Ashutosh Shukla, Subhankar Paul*
Identifiers and Pagination:Year: 2014
First Page: 6
Last Page: 15
Publisher ID: TOBIOIJ-8-6
Article History:Received Date: 21/09/2013
Revision Received Date: 29/11/2013
Acceptance Date: 29/11/2013
Electronic publication date: 31/12/2014
Collection year: 2014
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Hsp90α is a stress protein that acts as a molecular chaperone and is known to assist in the maturation, folding and stabilization of various cellular proteins known as ‘client proteins’. However, the factors that drive the interaction between Hsp90α and its client proteins are not well understood. In the present investigation, we predicted the basis of the different interaction of Hsp90α with both wild and mutant p53 and other client proteins. We have predicted that the presence of hydrophobic patches having substantial value of hydropathy index and a minimum percent similarity of hydrophobic patches between Hsp90α and its client proteins of 40 % is a necessary condition for client proteins to be recognized by Hsp90α. We also predicted that the overall percentage hydrophobicity of client proteins more than 20 is a required condition for them to bind with Hsp90α. The docking energy of p53 with Hsp90α and with multi-chaperone complex was also separately reported. We have reported from docking result that mutant p53 has a stronger interaction with Hsp90 when associated with multi-chaperone complex than wild type p53 and this might be one of the causes of breast cancer pathogenesis.