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. 2021 May 18;16(16):2524–2534. doi: 10.1002/cmdc.202100246

Figure 3.

Figure 3

DENV‐3 protease conformational states. A) State I, a tightly closed state, is only seen with the ligand covalently bound system. B) State II, a semi‐closed state, where the NS3’s N‐terminal is unfolded. C) State III, the semi‐closed state where NS3’s N‐terminal is losing the beta‐sheet fold, but remains near the core protein D) State IV, fully open with the NS2B's C‐terminal uncovers the active site. The frequency of each conformation for covalent bound ligan (Cov), non‐covalent bound ligand (Non‐Cov) and apostructure (Apo) is shown below the structural representation. The grey cartoon represents the NS3 protease domain and light blue represents the NS2B, yellow spheres represent the position of the active site and relevant residues are depicted as sticks. E) box plot representation of the distance variation along the analysed trajectory and plotted by each cluster for relevant amino‐acid pairs. Lys73‐Asp80 was chosen to represent the charge‐clamp holding the NS2B in the closed conformation. Arg85‐Asp81 distance variation represents the NS2B's hairpin bending and conformational changes and Tyr150‐Tyr161 describes hydrophobic pair relevant for the NS3 folding.