Download MendeleyThe mechanism of H171T resistance reveals the importance of N -protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.
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.(2014) Retrovirology 11: 100-100
- PubMed: 25421939
- DOI: https://doi.org/10.1186/s12977-014-0100-1
- Primary Citation of Related Structures:
4TSX - 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.
Organizational Affiliation:
Center for Retrovirus Research and Comprehensive Cancer Center, College of Pharmacy, The Ohio State University, 496 W. 12th Ave, 508 Riffe Building, Columbus, OH, 43210, USA. slaughter.89@osu.edu.
