3BWK
Crystal Structure of Falcipain-3 with Its inhibitor, K11017
Summary for 3BWK
| Entry DOI | 10.2210/pdb3bwk/pdb |
| Related | 1AIM 1YVB 2GHU 3BPF 3BPM |
| Descriptor | Cysteine protease falcipain-3, N~2~-(morpholin-4-ylcarbonyl)-N-[(3S)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-leucinamide, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | falcipain, malaria, cysteine protease, hydrolase |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 4 |
| Total formula weight | 112101.40 |
| Authors | Kerr, I.,Lee, J.H.,Brinen, L.S. (deposition date: 2008-01-09, release date: 2009-01-20, Last modification date: 2024-11-20) |
| Primary citation | Kerr, I.D.,Lee, J.H.,Farady, C.J.,Marion, R.,Rickert, M.,Sajid, M.,Pandey, K.C.,Caffrey, C.R.,Legac, J.,Hansell, E.,McKerrow, J.H.,Craik, C.S.,Rosenthal, P.J.,Brinen, L.S. Vinyl sulfones as antiparasitic agents and a structural basis for drug design. J.Biol.Chem., 284:25697-25703, 2009 Cited by PubMed Abstract: Cysteine proteases of the papain superfamily are implicated in a number of cellular processes and are important virulence factors in the pathogenesis of parasitic disease. These enzymes have therefore emerged as promising targets for antiparasitic drugs. We report the crystal structures of three major parasite cysteine proteases, cruzain, falcipain-3, and the first reported structure of rhodesain, in complex with a class of potent, small molecule, cysteine protease inhibitors, the vinyl sulfones. These data, in conjunction with comparative inhibition kinetics, provide insight into the molecular mechanisms that drive cysteine protease inhibition by vinyl sulfones, the binding specificity of these important proteases and the potential of vinyl sulfones as antiparasitic drugs. PubMed: 19620707DOI: 10.1074/jbc.M109.014340 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.42 Å) |
Structure validation
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