Computational Modeling of Allosteric Regulation in the Hsp90 Chaperones: A Statistical Ensemble Analysis of Protein Structure Networks and Allosteric Communications
Figure 8
Structural Maps of Stable Interaction Communities in the Hsp90 Structures.
The distribution of structurally stable interaction communities is shown for the SAXS structure of HtpG (A); the crystal structure of apo HtpG (B); the crystal structure of ADP-HtpG (C); and the crystal structure of yeast ATP-Hsp90 (D). The Hsp90 structures are shown in a ribbon representation and colored according to their domain nomenclature: Hsp90-NTD (in green), Hsp90-MD (in blue), and Hsp90-CTD (in red). The Hsp90 residues that constitute structural communities are shown in spheres and colored according to their respective domains. The residue-based annotation of stable communities is provided and structural positions of communities are indicated by arrows. Structural mapping of stable communities in the solution HtpG structure (A) and ADP-HtpG structure (C) shows a partly disjointed pattern of the interaction networks that are mostly confined within the individual domains. The ATP-bound dimer of yeast Hsp90 has a dense interaction network that includes both the inter-domain and the inter-monomer communities. The Pymol program was used for visualization of the Hsp90 structures (The PyMOL Molecular Graphics System, Version 1.2r3pre, Schrödinger, LLC).