Modeling Signal Propagation Mechanisms and Ligand-Based Conformational Dynamics of the Hsp90 Molecular Chaperone Full-Length Dimer
Figure 6
Structural representation of the N-terminal interface.
The structures represent the most populated conformations obtained from the cluster analysis of the liganded dimers. The interface residues involved in hydrophobic packing are highlighted with a sphere representation (residues 22, 23, 24, 376, 378, 380). In the presence of ATP the interface becomes tighter during the simulation (A). In the ADP simulation the hydrophobic packing is disrupted (B).