4TSX

HIV-1 Integrase Catalytic Core Domain Mutant Complexed with Allosteric Inhibitor

4TSX の概要

• エントリーDOI: 10.2210/pdb4tsx/pdb
• 関連するPDBエントリー: 1ITG
• 分子名称: Integrase, (2S)-tert-butoxy[4-(3,4-dihydro-2H-chromen-6-yl)-2-methylquinolin-3-yl]ethanoic acid, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hiv integrase, ccd, h171t, dde motif, dimer interface, allosteric inhibitor, allini, quinoline, dna binding protein
• 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: 18713.01

構造登録者

Feng, L.,Kvaratskhelia, M. (登録日: 2014-06-19, 公開日: 2014-12-17, 最終更新日: 2024-11-13)

主引用文献

Slaughter, A.,Jurado, K.A.,Deng, N.,Feng, L.,Kessl, J.J.,Shkriabai, N.,Larue, R.C.,Fadel, H.J.,Patel, P.A.,Jena, N.,Fuchs, J.R.,Poeschla, E.,Levy, R.M.,Engelman, A.,Kvaratskhelia, M.
The mechanism of H171T resistance reveals the importance of N -protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.
Retrovirology, 11:100-100, 2014

PubMed Abstract: Allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) are an important new class of anti-HIV-1 agents. ALLINIs bind at the IN catalytic core domain (CCD) dimer interface occupying the principal binding pocket of its cellular cofactor LEDGF/p75. Consequently, ALLINIs inhibit HIV-1 IN interaction with LEDGF/p75 as well as promote aberrant IN multimerization. Selection of viral strains emerging under the inhibitor pressure has revealed mutations at the IN dimer interface near the inhibitor binding site.

PubMed: 25421939
DOI: 10.1186/s12977-014-0100-1

実験手法

X-RAY DIFFRACTION (1.94 Å)