The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase

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...

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Veröffentlicht in:	Retrovirology 2014-11, Vol.11 (1), p.100, Article 100
Hauptverfasser:	Slaughter, Alison, Jurado, Kellie A, Deng, Nanjie, Feng, Lei, Kessl, Jacques J, Shkriabai, Nikoloz, Larue, Ross C, Fadel, Hind J, Patel, Pratiq A, Jena, Nivedita, Fuchs, James R, Poeschla, Eric, Levy, Ronald M, Engelman, Alan, Kvaratskhelia, Mamuka
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetates - metabolism Cell Line Crystallography, X-Ray Drug Resistance, Viral Histidine - genetics Histidine - metabolism HIV Integrase - chemistry HIV Integrase - genetics HIV Integrase - metabolism HIV Integrase Inhibitors - metabolism HIV-1 - drug effects HIV-1 - enzymology Humans Models, Molecular Mutant Proteins - chemistry Mutant Proteins - genetics Mutant Proteins - metabolism Mutation, Missense Protein Binding Protein Conformation Quinolines - metabolism
Online-Zugang:	Volltext
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