1AJV

HIV-1 PROTEASE IN COMPLEX WITH THE CYCLIC SULFAMIDE INHIBITOR AHA006

Summary for 1AJV

• Entry DOI: 10.2210/pdb1ajv/pdb
• Descriptor: HIV-1 PROTEASE, 2,7-DIBENZYL-1,1-DIOXO-3,6-BIS-PHENOXYMETHYL-[1,2,7]THIADIAZEPANE-4,5-DIOL (3 entities in total)
• Functional Keywords: protease, aspartyl protease, non-peptide inhibitor, drug design, hiv-1
• Biological source: Human immunodeficiency virus 1
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03366
• Total number of polymer chains: 2
• Total formula weight: 22182.20

Authors

Backbro, K.,Unge, T. (deposition date: 1997-05-11, release date: 1997-08-20, Last modification date: 2024-05-22)

Primary citation

Backbro, K.,Lowgren, S.,Osterlund, K.,Atepo, J.,Unge, T.,Hulten, J.,Bonham, N.M.,Schaal, W.,Karlen, A.,Hallberg, A.
Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.
J.Med.Chem., 40:898-902, 1997

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.

PubMed: 9083478
DOI: 10.1021/jm960588d

Experimental method

X-RAY DIFFRACTION (2 Å)