3L3U
Crystal structure of the HIV-1 integrase core domain to 1.4A
Summary for 3L3U
Entry DOI | 10.2210/pdb3l3u/pdb |
Related | 1bl3 1ex4 3L3V |
Descriptor | POL polyprotein, SULFATE ION (3 entities in total) |
Functional Keywords | dna integration, aids, integrase, endonuclease, polynucleotidyl transferase, dna binding, viral protein |
Biological source | Human immunodeficiency virus 1 |
Total number of polymer chains | 2 |
Total formula weight | 35892.54 |
Authors | Wielens, J.,Chalmers, D.K.,Scanlon, M.J.,Parker, M.W. (deposition date: 2009-12-17, release date: 2010-03-31, Last modification date: 2023-11-01) |
Primary citation | Wielens, J.,Headey, S.J.,Jeevarajah, D.,Rhodes, D.I.,Deadman, J.,Chalmers, D.K.,Scanlon, M.J.,Parker, M.W. Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site. Febs Lett., 584:1455-1462, 2010 Cited by PubMed 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. PubMed: 20227411DOI: 10.1016/j.febslet.2010.03.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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