Fig. 2
From: Protein conformational flexibility modulates kinetics and thermodynamics of drug binding
Comparison of different conformations of N-HSP90. a Overlay of three N-HSP90 crystal structures in complex with compounds 1 (black), 20 (red) and geldanamycin (wheat, PDB 1YET), representing loop-in, helical and loop-out conformations, respectively. The protein structures are shown in gray except α-helix3 (residues 101–123) and the lid segment (residues 107–141). A detailed view of the different conformations of α-helix3 is given in the inset. b Protein-ligand interactions representative of the loop-in conformation (compound 1). c Protein-ligand interactions representative of the helical conformation (compound 20). Dashed lines indicate interactions (blue: hydrogen bonds, yellow: aromatic, brown: hydrophobic). 2Fo-Fc electron density maps, contoured at 1.5σ, are shown in gray around each ligand
