Computational Modeling of Allosteric Regulation in the Hsp90 Chaperones: A Statistical Ensemble Analysis of Protein Structure Networks and Allosteric Communications
Figure 2
Conformational Dynamics of the Hsp90 Crystal Structures.
The computed B-factors are obtained from MD simulations of apo-HtpG [56] (PDB ID 2IOQ) (A); ADP-bound HtpG [56] (PDB ID 2IOP) (B); ATP-bound yeast Hsp90 [55] (PDB ID 2CG9) (C); and ATP-bound Grp94 [61] (PDB ID 2O1U) (D). The NTD residues are shown in green, MD residues are in blue, and CTD residues are in red. The residue-based profiles are based on the consecutive residue numbering adopted from the original crystallographic residue annotation. For clarity, the equilibrium profiles are shown only for one monomer of the homodimer. (A) The fluctuation profile of the apo-HtpG crystal structure has the following residue annotation: NTD (residues 1–219); MD (residues 220–474); CTD (residues 475–577). (B) The profile of the ADP-HtpG crystal structure has the following residue annotation: NTD (residues 1–231); MD (residues 232–486); CTD (residues 487–618). (C) The force constant profile of the yeast ATP-Hsp90 has the following residue annotation: NTD (residues 1–215); MD (residues 216–471); CTD (residues 472–609). (D) The force constant profile of the ATP-Grp94 crystal structure has the following residue annotation: NTD (residues 1–179); MD (residues 180–427); CTD (residues 428–573).