1HIH
COMPARATIVE ANALYSIS OF THE X-RAY STRUCTURES OF HIV-1 AND HIV-2 PROTEASES IN COMPLEX WITH CGP 53820, A NOVEL PSEUDOSYMMETRIC INHIBITOR
1HIH の概要
エントリーDOI | 10.2210/pdb1hih/pdb |
分子名称 | HIV-1 PROTEASE, BETA-MERCAPTOETHANOL, ACETYL-NH-VAL-CYCLOHEXYL-CH2[NCH2CHOH]CH2-BENZYL-VAL-NH-ACETYL, ... (4 entities in total) |
機能のキーワード | aspartate protease, inhibited, hiv, hydrolase (aspartic proteinase) |
由来する生物種 | Human immunodeficiency virus 1 |
細胞内の位置 | 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 : P03366 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 22337.54 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 7613867DOI: 10.1016/S0969-2126(01)00169-1 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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