Modeling Signal Propagation Mechanisms and Ligand-Based Conformational Dynamics of the Hsp90 Molecular Chaperone Full-Length Dimer
Figure 7
Structural detail of the interface showing the difference between the ATP and the ADP simulation.
(A) In the presence of ATP the loop containing Y24 protrudes from one protomer to the other and the two tyrosines are pointing to each other. Helices 1, depicted in red in both protomers, are nearly parallel. (B) In the ADP simulation, Y24 of one protomer rotates away from the interface towards its nucleotide binding site, which results in an increased tilting of helices 1(in red) and a relative displacement of the other protomer.