3BPF
Crystal Structure of Falcipain-2 with Its inhibitor, E64
Summary for 3BPF
| Entry DOI | 10.2210/pdb3bpf/pdb |
| Related | 1AIM 1YVB 2GHU 3BPM |
| Descriptor | Cysteine protease falcipain-2, N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | falcipain, malaria, cysteine protease, hydrolase, thiol protease |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 4 |
| Total formula weight | 110280.50 |
| Authors | kerr, I.D.,Lee, J.H.,Brinen, L.S. (deposition date: 2007-12-18, release date: 2008-12-30, Last modification date: 2024-11-13) |
| Primary citation | Kerr, I.D.,Lee, J.H.,Pandey, K.C.,Harrison, A.,Sajid, M.,Rosenthal, P.J.,Brinen, L.S. Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity. J.Med.Chem., 52:852-857, 2009 Cited by PubMed Abstract: Falcipain-2 and falcipain-3 are critical hemoglobinases of Plasmodium falciparum, the most virulent human malaria parasite. We have determined the 2.9 A crystal structure of falcipain-2 in complex with the epoxysuccinate E64 and the 2.5 A crystal structure of falcipain-3 in complex with the aldehyde leupeptin. These complexes represent the first crystal structures of plasmodial cysteine proteases with small molecule inhibitors and the first reported crystal structure of falcipain-3. Our structural analyses indicate that the relative shape and flexibility of the S2 pocket are affected by a number of discrete amino acid substitutions. The cumulative effect of subtle differences, including those at "gatekeeper" positions, may explain the observed kinetic differences between these two closely related enzymes. PubMed: 19128015DOI: 10.1021/jm8013663 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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