Computational Modeling of Allosteric Regulation in the Hsp90 Chaperones: A Statistical Ensemble Analysis of Protein Structure Networks and Allosteric Communications
Figure 12
The Residue-Based Betweenness Profiles of the ATP-bound yeast Hsp90 and Grp94 Structures.
The residue-based betweenness profiles are shown for the crystal structure of yeast ATP-Hsp90 (A) and the crystal structure of ATP-Grp94 (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 crystal structure of yeast ATP-Hsp90 (B) and the crystal structure of ATP-Grp94 (D). The protein structures are shown in a backbone trace protein representation and colored according to their domain nomenclature as in Figure 11. The functional residues of high centrality are shown in spheres and colored according to their respective domains. Structural positions of high centrality residues are indicated by arrows.