3EJ5
complex of Ricin A chain and pyrimidine-based inhibitor
Summary for 3EJ5
| Entry DOI | 10.2210/pdb3ej5/pdb |
| Descriptor | Ricin A chain, 4-[3-(2-amino-4-hydroxy-6-oxo-1,6-dihydropyrimidin-5-yl)propyl]benzoic acid (3 entities in total) |
| Functional Keywords | protein inhibitor complex, glycoprotein, hydrolase, lectin, nucleotide-binding, plant defense, protein synthesis inhibitor, toxin |
| Biological source | Ricinus communis (Castor bean) |
| Total number of polymer chains | 1 |
| Total formula weight | 29051.70 |
| Authors | Bai, Y.,Monzingo, A.F.,Robertus, J.D. (deposition date: 2008-09-17, release date: 2009-04-07, Last modification date: 2023-08-30) |
| Primary citation | Bai, Y.,Monzingo, A.F.,Robertus, J.D. The X-ray structure of ricin A chain with a novel inhibitor Arch.Biochem.Biophys., 483:23-28, 2009 Cited by PubMed Abstract: Ricin is a potent heterodimeric cytotoxin; the B chain binds eucaryotic cell surfaces aiding uptake and the A chain, RTA, reaches the cytoplasm where it enzymatically depurinates a key ribosomal adenine, inhibiting protein synthesis. Ricin is known to be an agent in bioterrorist repertoires and there is great interest in finding, or creating, efficacious inhibitors of the toxin as potential antidotes. We have previously identified two families of bicyclic RTA inhibitors, pterins and purines. Both classes have poor solubility which impairs inhibitor development. Here we report the use of 2-amino-4,6-dihydroxy-pyrimidines as RTA inhibitors. Unlike previously observed single ring inhibitor platforms, these displace Tyr 80 and bind deep in the RTA specificity pocket. These compounds are at least 10 times more soluble than pterin-based inhibitors and appear to be useful new class of ricin inhibitors. PubMed: 19138659DOI: 10.1016/j.abb.2008.12.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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