Computational Modeling of Allosteric Regulation in the Hsp90 Chaperones: A Statistical Ensemble Analysis of Protein Structure Networks and Allosteric Communications
Figure 7
The Network Analysis of the Hsp90 Crystal Structures.
The distribution of hubs (A) and communities (B) in different functional states of Hsp90. The distributions of protein structure network parameters are obtained by averaging computations over MD simulation trajectories. The analysis is based on structurally stable residue interaction networks that remained intact in more than 75% of the simulation snapshots. The distributions are shown for the open solution conformation of HtpG obtained from SAXS studies [57], [58] (in blue); an apo form of HtpG (PDB ID 2IOQ) [56] (in red); an ADP-bound form of HtpG (PDB ID 2IOP) [56] (in green); an ADP-bound form of the Grp94 homologue (PDB ID 2O1V) [61] (in maroon); an ATP-bound form of the Grp94 homologue (PDB ID 2O1U) [61] (in orange); and an ATP-bound conformation of yeast Hsp90 (PDB ID 2CG9) [55] (in brown).