| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10337819 | Journal of Molecular Graphics and Modelling | 2011 | 9 Pages |
Abstract
⺠Comparative molecular dynamics simulations on HIV-1 IN bound with L-731,988, L-708,906 and S-1360. ⺠The acidic end of all the DKA inhibitors studied formed favourable ionic interactions with Lys159. ⺠The keto-enol parts of these compounds were consistently coordinated to Mg. ⺠The catalytic residue Glu152 formed a favourable ion-pair interaction with the negatively charged Arg199 on α6 in the most potent DKA inhibitors. ⺠The complexation with Merck inhibitors and S-1360 significantly constrained the flexible surface loop into an extended or open conformation.
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Authors
Meilan Huang, Guy H. Grant, W. Graham Richards,