Ionization states of the catalytic residues in HIV-1 protease

@article{Smith1996IonizationSO,
  title={Ionization states of the catalytic residues in HIV-1 protease},
  author={Ross Smith and I. Brereton and R. Y. Chai and S. Kent},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={946-950}
}
Chemical synthesis was used to prepare the HIV-1 protease specifically 13C-labelled in the catalytically essential Asp 25 in each monomer. The NMR chemical shift of the 13C-enriched homodimeric enzyme was measured in the presence of the inhibitor pepstatin, a mimic of the tetrahedral intermediate formed in enzyme catalysis. In this complex, the catalytic carboxyls do not titrate in the pH range where the enzyme is active; throughout the range pH 2.5–6.5, one Asp 25 side chain is protonated and… Expand
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Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high-resolution X-ray and neutron crystallography
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