Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.

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Citation

Backbro K, Lowgren S, Osterlund K, Atepo J, Unge T, Hulten J, Bonham NM, Schaal W, Karlen A, Hallberg A

Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.

J Med Chem. 1997 Mar 14;40(6):898-902.

PubMed ID
9083478 [ View in PubMed
]
Abstract

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 A 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Gag-Pol polyproteinP03366Details