Inhibitor-interaction, dimerization and activity change of HIV-1 protease mutants evolved under drug-pressure

Inhibitor-bound HIV-1 protease homodimer

A designates that the subunit that contains this residue is bound to the bis-THF side of the inhibitor.
B designates that the subunit that contains this residue is bound to the aniline side of the inhibitor.
If blank, the assignment to the bis-THF of aniline functional group part of the inhibitor is unknown.

(3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yl [(2S,3R)-4-{[(4-aminophenyl)sulfonyl](2-methylpropyl)amino}-3-hydroxy-1-phenylbutan-2-yl]carbamate

[(3R,3aS,6aR)-2,3,3a,4,5,6a-hexahydrofuro[2,3-b]furan-3-yl] N-[(2S,3R)-4-[(4-aminophenyl)sulfonyl-(2-methylpropyl)amino]-3-hydroxy-1-phenyl-butan-2-yl]carbamate

Protein science : a publication of the Protein Society
A synergy of activity, stability, and inhibitor-interaction of HIV-1 protease mutants evolved under drug-pressure.

5mm triple resonance, Z-axis gradient, cryoprobe

Backbone 1H, 13C, and 15N Chemical Shift Assignments of HIV-1 Protease (Flap + mutant) bound to Darunavir.

Backbone 1H, 13C, and 15N Chemical Shift Assignments of WT HIV-1 Protease bound to Darunavir.

Inhibitor-bound HIV-1 protease homodimer, I54A

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax