Unexpected Binding Mode of a Cyclic Sulfamide HIV-1 Protease Inhibitor

Autor: Backbro, K., Lowgren, S., Osterlund, K., Atepo, J., Unge, T., Hulten, J., Bonham, N. M., Schaal, W., Karlen, A., Hallberg, A.
Zdroj: Journal of Medicinal Chemistry; March 14, 1997, Vol. 40 Issue: 6 p898-902, 5p
Abstrakt: Two cyclic, C2-symmetric HIV-1 protease inhibitors, one sulfamide and one urea derivative, both comprising phenyl ether groups in the P1/P1‘ positions, were cocrystallized with HIV-1 protease, and the crystal structures were determined to 2.0 Å resolution. The structure of the urea 2 showed a conformation similar to that reported for the related urea 3 by Lam et al., while the sulfamide 1 adopted an unanticipated conformation in which the P1‘ and P2‘ side chains were transposed.
Databáze: Supplemental Index