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  • Title: Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site.
    Author: Wielens J, Headey SJ, Jeevarajah D, Rhodes DI, Deadman J, Chalmers DK, Scanlon MJ, Parker MW.
    Journal: FEBS Lett; 2010 Apr 16; 584(8):1455-62. PubMed ID: 20227411.
    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.
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