Probing Molecular Mechanisms of the Hsp90 Chaperone: Biophysical Modeling Identifies Key Regulators of Functional Dynamics
Figure 11
Structure-Functional Analysis of Allosteric Regulators in the Grp94 Chaperone.
(A) Structural mapping and overview of the functional regions corresponding to the stationary points in the NMSF profiles. The Pymol program was used for visualization of Hsp90 structures. The NTD residues are shown in blue, the M-domain residues are in yellow-greenish and the CTD residues are in pink. The Hsp90 structures are in ribbons overlayed with the surface representation at the 50% transparency according to PyMOL. (B) A close-up view of the M-domain regulatory motif (residues 444–454 LNVSRETLQQ from the M-domain). The functional motif is shown in cyan spheres depicting only the main chain amino acids. The catalytic residue Arg-448 is highlighted in red spheres. (C) A close-up view of the CTD functional regulatory region (residues 643-SPCAL-647). The functional region is shown in cyan spheres and the critical switch node residue Ala-646 is shown in red spheres.