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4Z4X

Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20D25N with Open Flap

4Z4X の概要
エントリーDOI10.2210/pdb4z4x/pdb
関連するPDBエントリー4Z50
分子名称Protease (2 entities in total)
機能のキーワードhiv-1 protease, hydrolase
由来する生物種Human immunodeficiency virus 1
タンパク質・核酸の鎖数2
化学式量合計21531.12
構造登録者
Chang, Y.C.,Shen, C.-H.,Weber, I.T. (登録日: 2015-04-02, 公開日: 2015-10-14, 最終更新日: 2023-09-27)
主引用文献Shen, C.H.,Chang, Y.C.,Agniswamy, J.,Harrison, R.W.,Weber, I.T.
Conformational variation of an extreme drug resistant mutant of HIV protease.
J.Mol.Graph.Model., 62:87-96, 2015
Cited by
PubMed Abstract: Molecular mechanisms leading to high level drug resistance have been analyzed for the clinical variant of HIV-1 protease bearing 20 mutations (PR20); which has several orders of magnitude worse affinity for tested drugs. Two crystal structures of ligand-free PR20 with the D25N mutation of the catalytic aspartate (PR20D25N) revealed three dimers with different flap conformations. The diverse conformations of PR20D25N included a dimer with one flap in a unique "tucked" conformation; directed into the active site. Analysis of molecular dynamics (MD) simulations of the ligand-free PR20 and wild-type enzymes showed that the mutations in PR20 alter the correlated interactions between two monomers in the dimer. The two flaps tend to fluctuate more independently in PR20 than in the wild type enzyme. Combining the results of structural analysis by X-ray crystallography and MD simulations; unusual flap conformations and weakly correlated inter-subunit motions may contribute to the high level resistance of PR20.
PubMed: 26397743
DOI: 10.1016/j.jmgm.2015.09.006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.75 Å)
構造検証レポート
Validation report summary of 4z4x
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-08-06に公開中

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