2Q3K
Crystal Structure of Lysine Sulfonamide Inhibitor Reveals the Displacement of the Conserved Flap Water Molecule in HIV-1 Protease
Summary for 2Q3K
| Entry DOI | 10.2210/pdb2q3k/pdb |
| Descriptor | Protease, PHOSPHATE ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | drug design, hiv-1 protease, protease inhibitors, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 2 |
| Total formula weight | 22637.47 |
| Authors | Schiffer, C.A.,Nalam, M.N.L. (deposition date: 2007-05-30, release date: 2007-08-21, Last modification date: 2023-08-30) |
| Primary citation | Nalam, M.N.,Peeters, A.,Jonckers, T.H.,Dierynck, I.,Schiffer, C.A. Crystal structure of lysine sulfonamide inhibitor reveals the displacement of the conserved flap water molecule in human immunodeficiency virus type 1 protease. J.Virol., 81:9512-9518, 2007 Cited by PubMed Abstract: Human immunodeficiency virus type 1 (HIV-1) protease has been continuously evolving and developing resistance to all of the protease inhibitors. This requires the development of new inhibitors that bind to the protease in a novel fashion. Most of the inhibitors that are on the market are peptidomimetics, where a conserved water molecule mediates hydrogen bonding interactions between the inhibitors and the flaps of the protease. Recently a new class of inhibitors, lysine sulfonamides, was developed to combat the resistant variants of HIV protease. Here we report the crystal structure of a lysine sulfonamide. This inhibitor binds to the active site of HIV-1 protease in a novel manner, displacing the conserved water and making extensive hydrogen bonds with every region of the active site. PubMed: 17596316DOI: 10.1128/JVI.00799-07 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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