1LV1

Crystal Structure Analysis of the non-active site mutant of tethered HIV-1 protease to 2.1A resolution

1LV1 の概要

• エントリーDOI: 10.2210/pdb1lv1/pdb
• 関連するPDBエントリー: 1G6L
• 分子名称: HIV-1 protease (2 entities in total)
• 機能のキーワード: beta-ribbon flap, hydrolase
• 由来する生物種: Human immunodeficiency virus 1; 詳細
• 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 : P04585
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21902.76

構造登録者

Kumar, M.,Kannan, K.K.,Hosur, M.V.,Bhavesh, N.S.,Chatterjee, A.,Mittal, R.,Hosur, R.V. (登録日: 2002-05-24, 公開日: 2002-06-19, 最終更新日: 2024-05-29)

主引用文献

Kumar, M.,Kannan, K.K.,Hosur, M.V.,Bhavesh, N.S.,Chatterjee, A.,Mittal, R.,Hosur, R.V.
Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations.
Biochem.Biophys.Res.Commun., 294:395-401, 2002

PubMed Abstract: Autolysis rates of the C95M and C95M/C1095A mutants of a HIV-1 protease tethered dimer have been determined by real time NMR and it is observed that the double mutant has approximately two times higher rate. X-ray structure of the C95M/C1095A double mutant has been solved and refined to 2.1 A resolution. Comparison of the double mutant structure with that of C95M single mutant reveals that there is a shift in the position of the catalytic aspartates and the bound catalytic water. The mutation also causes a loss of hydrophobic packing near the dimerization domain of the protein. These observations demonstrate that subtle changes are adequate to cause significant changes in the rate of autolysis of the double mutant. This provides a rationale for the effects of remote mutations on the activity and drug resistance of the enzyme.

PubMed: 12051725
DOI: 10.1016/S0006-291X(02)00482-5

実験手法

X-RAY DIFFRACTION (2.1 Å)