1A5W

ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3

1A5W の概要

• エントリーDOI: 10.2210/pdb1a5w/pdb
• 分子名称: INTEGRASE, 4-ACETYLAMINO-5-HYDROXYNAPHTHALENE-2,7-DISULFONIC ACID (3 entities in total)
• 機能のキーワード: hydrolase, endonuclease, hiv-1 integrase inhibitor
• 由来する生物種: Rous sarcoma virus (strain Schmidt-Ruppin)
• 細胞内の位置: Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03354
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17760.27

構造登録者

Lubkowski, J.,Yang, F.,Alexandratos, J.,Wlodawer, A. (登録日: 1998-02-18, 公開日: 1998-05-27, 最終更新日: 2024-05-22)

主引用文献

Lubkowski, J.,Yang, F.,Alexandratos, J.,Wlodawer, A.,Zhao, H.,Burke Jr., T.R.,Neamati, N.,Pommier, Y.,Merkel, G.,Skalka, A.M.
Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor.
Proc.Natl.Acad.Sci.USA, 95:4831-4836, 1998

PubMed Abstract: The x-ray structures of an inhibitor complex of the catalytic core domain of avian sarcoma virus integrase (ASV IN) were solved at 1.9- to 2.0-A resolution at two pH values, with and without Mn2+ cations. This inhibitor (Y-3), originally identified in a screen for inhibitors of the catalytic activity of HIV type 1 integrase (HIV-1 IN), was found in the present study to be active against ASV IN as well as HIV-1 IN. The Y-3 molecule is located in close proximity to the enzyme active site, interacts with the flexible loop, alters loop conformation, and affects the conformations of active site residues. As crystallized, a Y-3 molecule stacks against its symmetry-related mate. Preincubation of IN with metal cations does not prevent inhibition, and Y-3 binding does not prevent binding of divalent cations to IN. Three compounds chemically related to Y-3 also were investigated, but no binding was observed in the crystals. Our results identify the structural elements of the inhibitor that likely determine its binding properties.

PubMed: 9560188
DOI: 10.1073/pnas.95.9.4831

実験手法

X-RAY DIFFRACTION (2 Å)