1HVC

CRYSTAL STRUCTURE OF A TETHERED DIMER OF HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR

1HVC の概要

• エントリーDOI: 10.2210/pdb1hvc/pdb
• 分子名称: HIV-1 PROTEASE, N-{1-BENZYL-(2S,3S)-2,3-DIHYDROXY-4-[3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRYLAMINO]-5-PHENYL-PENTYL}-3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRAMIDE (3 entities in total)
• 機能のキーワード: hydrolase(acid protease)
• 由来する生物種: Human immunodeficiency virus 1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22756.83

構造登録者

Bhat, T.N.,Baldwin, E.T.,Erickson, J.W. (登録日: 1994-06-22, 公開日: 1994-10-15, 最終更新日: 2024-02-07)

主引用文献

Bhat, T.N.,Baldwin, E.T.,Liu, B.,Cheng, Y.S.,Erickson, J.W.
Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor.
Nat.Struct.Biol., 1:552-556, 1994

PubMed Abstract: HIV-1 proteinase (HIV PR) is a dimeric enzyme composed of two identical polypeptide chains that associate with twofold symmetry. We have determined to 1.8 A the crystal structure of a covalently tethered dimer of HIV PR. The tethered dimer:inhibitor complex is identical in nearly every respect to the complex of the same inhibitor with the wild type dimeric molecule, except for the linker region. Our results suggest that the tethered dimer may be a useful surrogate enzyme for studying the effects of single site mutations on substrate and inhibitor binding as well as on enzyme asymmetry, and for simulating independent mutational drift of the two domains which has been proposed to have led to the evolution of modern day, single-chain aspartic proteinases.

PubMed: 7664084
DOI: 10.1038/nsb0894-552

実験手法

X-RAY DIFFRACTION (1.8 Å)