Structural Bioinformatics and Protein Docking Analysis of the Molecular Chaperone-Kinase Interactions: Towards Allosteric Inhibition of Protein Kinases by Targeting the Hsp90-Cdc37 Chaperone Machinery

Structural Bioinformatics and Protein Docking Analysis of the Molecular Chaperone-Kinase Interactions: Towards Allosteric Inhibition of Protein Kinases by Targeting the Hsp90-Cdc37 Chaperone Machinery

A fundamental role of the Hsp90-Cdc37 chaperone system in mediating maturation of protein kinase clients and supporting kinase functional activity is essential for the integrity and viability of signaling pathways involved in cell cycle control and organism development. Despite significant advances...

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Bibliographic Details
Main Authors: Gennady Verkhivker, Elizabeth Berrigan, Nathan Lawless, Kristin Blacklock
Format: Article
Language:English
Published: MDPI AG 2013-11-01
Series:Pharmaceuticals
Subjects:
molecular chaperones
protein kinases
protein docking
protein-protein interactions
allosteric binding sites
drug discovery
Online Access:http://www.mdpi.com/1424-8247/6/11/1407

Internet

http://www.mdpi.com/1424-8247/6/11/1407

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