Computational Modeling of Allosteric Regulation in the Hsp90 Chaperones: A Statistical Ensemble Analysis of Protein Structure Networks and Allosteric Communications
Figure 11
The Residue-Based Betweenness Profiles of the HtpG Structures.
Dynamics-based analysis of network centrality in the HtpG crystal structures. The residue-based betweenness profiles are shown for the apo HtpG crystal structure (A) and the ADP-HtpG crystal structure (C). The betweenness profiles are shown in green for the NTD residues, in blue for the MD residues, and in red for the CTD residues. The peaks of the betweenness profiles corresponding to functionally important residues are indicated by arrows and annotated. Structural mapping of high betweenness residues that correspond to functionally important sites is shown for the apo HtpG crystal structure (B) and the ADP-HtpG crystal structure (D). The protein structures are shown in a backbone trace representation and domain-colored: NTD (in green), MD (in blue), and CTD (in red). The functional residues of high centrality are shown in spheres and colored according to their respective domains. Structural positions of high centrality functional residues are indicated by arrows.