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. 2013 Nov 11;6(11):1407–1428. doi: 10.3390/ph6111407

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© 2013 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

PMC Copyright notice

Structures and Energies of the Hsp90-Cdc37-Cdk4 Docked Complexes. The presented docked solutions are the low-energy binding modes obtained after stages of 3-body docking, refinement and clustering. Structures of the Hsp90-Cdc37-Cdk4 complexes are aligned with their respective HADDOCK score. A surface-based protein representation is used. The Hsp90 dimer is shown in green, Cdc37 is colored in red and Cdk4 is displayed in blue. Structural analysis of the docked solutions shows a gradual improvement and consolidation of the Hsp90-Cdc37 and Cdc37-Cdk4 intermolecular interfaces as the HADDOCK score of the docked complexes improved.