2R5P

Crystal Structure Analysis of HIV-1 Subtype C Protease Complexed with Indinavir

2R5P の概要

• エントリーDOI: 10.2210/pdb2r5p/pdb
• 関連するPDBエントリー: 2R5Q
• 分子名称: Protease, CHLORIDE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: hiv-1 subtype c, aspartyl protease, hydrolase, protease, viral protein
• 由来する生物種: Human immunodeficiency virus 1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44399.53

構造登録者

Coman, R.M.,Robbins, A.H.,McKenna, R.,Dunn, B.M. (登録日: 2007-09-04, 公開日: 2007-11-20, 最終更新日: 2024-02-21)

主引用文献

Coman, R.M.,Robbins, A.H.,Fernandez, M.A.,Gilliland, C.T.,Sochet, A.A.,Goodenow, M.M.,McKenna, R.,Dunn, B.M.
The Contribution of Naturally Occurring Polymorphisms in Altering the Biochemical and Structural Characteristics of HIV-1 Subtype C Protease
Biochemistry, 47:731-743, 2008

PubMed Abstract: Fourteen subtype B and C protease variants have been engineered in an effort to study whether the preexistent baseline polymorphisms, by themselves or in combination with drug resistance mutations, differentially alter the biochemical and structural features of the subtype C protease when compared with those of subtype B protease. The kinetic studies performed in this work showed that the preexistent polymorphisms in subtype C protease, by themselves, do not provide for a greater level of resistance. Inhibition analysis with eight clinically used protease inhibitors revealed that the natural polymorphisms found in subtype C protease, in combination with drug resistance mutations, can influence enzymatic catalytic efficiency and inhibitor resistance. Structural analyses of the subtype C protease bound to nelfinavir and indinavir showed that these inhibitors form similar interactions with the residues in the active site of subtype B and C proteases. It also revealed that the naturally occurring polymorphisms could alter the position of the outer loops of the subtype C protease, especially the 60's loop.

PubMed: 18092815
DOI: 10.1021/bi7018332

実験手法

X-RAY DIFFRACTION (2.3 Å)