Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
Baldwin, E.T., Bhat, T.N., Gulnik, S., Liu, B., Topol, I.A., Kiso, Y., Mimoto, T., Mitsuya, H., Erickson, J.W.(1995) Structure 3: 581-590
- PubMed: 8590019 
- DOI: https://doi.org/10.1016/s0969-2126(01)00192-7
- Primary Citation of Related Structures:  
1HPX - PubMed Abstract: 
HIV-1 protease (HIV PR), an aspartic protease, cleaves Phe-Pro bonds in the Gag and Gag-Pol viral polyproteins. Substrate-based peptide mimics constitute a major class of inhibitors of HIV PR presently being developed for AIDS treatment. One such compound, KNI-272, which incorporates allophenylnorstatine (Apns)-thioproline (Thp) in place of Phe-Pro, has potent antiviral activity and is undergoing clinical trials. The structure of the enzyme-inhibitor complex should lead to an understanding of the structural basis for its tight binding properties and provide a framework for interpreting the emerging resistance to this drug.
Organizational Affiliation: 
Frederick Biomedical Supercomputing Center, SAIC-Frederick, NCI-Frederick Cancer Research and Development Center, Maryland 21702, USA.