1HII

COMPARATIVE ANALYSIS OF THE X-RAY STRUCTURES OF HIV-1 AND HIV-2 PROTEASES IN COMPLEX WITH CGP 53820, A NOVEL PSEUDOSYMMETRIC INHIBITOR

Summary for 1HII

• Entry DOI: 10.2210/pdb1hii/pdb
• Descriptor: HIV-2 PROTEASE, SULFATE ION, ACETYL-NH-VAL-CYCLOHEXYL-CH2[NCH2CHOH]CH2-BENZYL-VAL-NH-ACETYL, ... (4 entities in total)
• Functional Keywords: aspartate protease, inhibited, hiv, hydrolase (aspartic proteinase)
• Biological source: Human immunodeficiency virus 2
• Cellular location: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P04584
• Total number of polymer chains: 2
• Total formula weight: 22222.57

Authors

Priestle, J.P.,Gruetter, M.G. (deposition date: 1995-03-31, release date: 1995-07-10, Last modification date: 2024-02-07)

Primary citation

Priestle, J.P.,Fassler, A.,Rosel, J.,Tintelnot-Blomley, M.,Strop, P.,Grutter, M.G.
Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor.
Structure, 3:381-389, 1995

PubMed Abstract: The human immunodeficiency virus (HIV) is the causative agent of acquired immunodeficiency syndrome (AIDS). Two subtypes of the virus, HIV-1 and HIV-2, have been characterized. The protease enzymes from these two subtypes, which are aspartic acid proteases and have been found to be essential for maturation of the infectious particle, share about 50% sequence identity. Differences in substrate and inhibitor binding between these enzymes have been previously reported.

PubMed: 7613867
DOI: 10.1016/S0969-2126(01)00169-1

Experimental method

X-RAY DIFFRACTION (2.3 Å)