3KHJ
C. parvum inosine monophosphate dehydrogenase bound by inhibitor C64
Summary for 3KHJ
| Entry DOI | 10.2210/pdb3khj/pdb |
| Related | 1LRT 1NF7 1NFB 1PVN 1ZFJ |
| Descriptor | Inosine-5-monophosphate dehydrogenase, INOSINIC ACID, N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide, ... (5 entities in total) |
| Functional Keywords | enzyme-inhibitor complex, oxidoreductase |
| Biological source | Cryptosporidium parvum More |
| Total number of polymer chains | 8 |
| Total formula weight | 312216.09 |
| Authors | MacPherson, I.S.,Hedstrom, L.K. (deposition date: 2009-10-30, release date: 2010-02-02, Last modification date: 2024-02-21) |
| Primary citation | Macpherson, I.S.,Kirubakaran, S.,Gorla, S.K.,Riera, T.V.,D'Aquino, J.A.,Zhang, M.,Cuny, G.D.,Hedstrom, L. The structural basis of Cryptosporidium -specific IMP dehydrogenase inhibitor selectivity. J.Am.Chem.Soc., 132:1230-1231, 2010 Cited by PubMed Abstract: Cryptosporidium parvum is a potential biowarfare agent, an important AIDS pathogen, and a major cause of diarrhea and malnutrition. No vaccines or effective drug treatment exist to combat Cryptosporidium infection. This parasite relies on inosine 5'-monophosphate dehydrogenase (IMPDH) to obtain guanine nucleotides, and inhibition of this enzyme blocks parasite proliferation. Here, we report the first crystal structures of CpIMPDH. These structures reveal the structural basis of inhibitor selectivity and suggest a strategy for further optimization. Using this information, we have synthesized low-nanomolar inhibitors that display 10(3) selectivity for the parasite enzyme over human IMPDH2. PubMed: 20052976DOI: 10.1021/ja909947a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
