3NXE

X-ray structure of ester chemical analogue 'covalent dimer' [Ile50,O-Ile50']HIV-1 protease complexed with MVT-101 inhibitor

3NXE の概要

• エントリーDOI: 10.2210/pdb3nxe/pdb
• 関連するPDBエントリー: 3FSM 3HAU 3HDK 3HLO 3NWQ 3NWX 3NXN 3NYG
• 関連するBIRD辞書のPRD_ID: PRD_000398
• 分子名称: protease covalent dimer, N-{(2S)-2-[(N-acetyl-L-threonyl-L-isoleucyl)amino]hexyl}-L-norleucyl-L-glutaminyl-N~5~-[amino(iminio)methyl]-L-ornithinamide, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: beta-barrel, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23047.87

構造登録者

Torbeev, V.Y.,Kent, S.B.H. (登録日: 2010-07-13, 公開日: 2011-11-02, 最終更新日: 2025-03-26)

主引用文献

Torbeev, V.Y.,Raghuraman, H.,Hamelberg, D.,Tonelli, M.,Westler, W.M.,Perozo, E.,Kent, S.B.
Protein conformational dynamics in the mechanism of HIV-1 protease catalysis.
Proc.Natl.Acad.Sci.USA, 108:20982-20987, 2011

PubMed Abstract: We have used chemical protein synthesis and advanced physical methods to probe dynamics-function correlations for the HIV-1 protease, an enzyme that has received considerable attention as a target for the treatment of AIDS. Chemical synthesis was used to prepare a series of unique analogues of the HIV-1 protease in which the flexibility of the "flap" structures (residues 37-61 in each monomer of the homodimeric protein molecule) was systematically varied. These analogue enzymes were further studied by X-ray crystallography, NMR relaxation, and pulse-EPR methods, in conjunction with molecular dynamics simulations. We show that conformational isomerization in the flaps is correlated with structural reorganization of residues in the active site, and that it is preorganization of the active site that is a rate-limiting factor in catalysis.

PubMed: 22158985
DOI: 10.1073/pnas.1111202108

実験手法

X-RAY DIFFRACTION (1.61 Å)