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Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site |
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| Authors: | Jerome Wielens Stephen J Headey David I Rhodes David K Chalmers Michael W Parker |
| Institution: | a Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, 381 Royal Parade, Parkville, Victoria 3052, Australia b Structural Biology Laboratory, St. Vincent’s Institute, 9 Princes Street, Fitzroy, Victoria 3065, Australia c Avexa Ltd., 576 Swan Street Richmond, Victoria 3121, Australia d Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 30 Flemington Road, Parkville, Victoria 3010, Australia |
| 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 summaryMINT-7713125: IN (uniprotkb:P04585) and IN (uniprotkb:P04585) bind (MI:0407) by X-ray crystallography (MI:0114) |
| Keywords: | Anti-HIV drug Ligand binding HIV-1 integrase X-ray crystallography |
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