Abstract
HIV integrase (IN) is an essential enzyme in HIV replication and an important target for drug design. IN has been shown to interact with a number of cellular and viral proteins during the integration process. Disruption of these important interactions could provide a mechanism for allosteric inhibition of IN. We present the highest resolution crystal structure of the IN core domain to date. We also present a crystal structure of the IN core domain in complex with sucrose which is bound at the dimer interface in a region that has previously been reported to bind integrase inhibitors. Structured summary MINT- 7713125: IN (uniprotkb: P04585) and IN (uniprotkb: P04585) bind (MI: 0407) by X-ray crystallography (MI: 0114)
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