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-Structure paper
Title | The mechanism of H171T resistance reveals the importance of N -protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase. |
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Journal, issue, pages | Retrovirology, Vol. 11, Page 100-100, Year 2014 |
Publish date | Jun 19, 2014 (structure data deposition date) |
Authors | 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. ...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. |
External links | Retrovirology / PubMed:25421939 |
Methods | X-ray diffraction |
Resolution | 1.94 Å |
Structure data | PDB-4tsx: |
Chemicals | ChemComp-LF0: ChemComp-SO4: ChemComp-HOH: |
Source |
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Keywords | DNA BINDING PROTEIN / HIV Integrase / CCD / H171T / DDE motif / dimer interface / allosteric inhibitor / ALLINI / quinoline |