1IL4
STRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 9-DEAZAGUANINE
Summary for 1IL4
| Entry DOI | 10.2210/pdb1il4/pdb |
| Related | 1BR5 1BR6 1FMP 1IL3 1IL5 1IL9 1RTC |
| Descriptor | RICIN A CHAIN, 9-DEAZAGUANINE (3 entities in total) |
| Functional Keywords | structure-based design, toxin-inhibitor complex, glycosidase, hydrolase, ribosome-inhibiting protein |
| Biological source | Ricinus communis (castor bean) |
| Total number of polymer chains | 1 |
| Total formula weight | 30086.90 |
| Authors | Miller, D.J.,Ravikumar, K.,Shen, H.,Suh, J.-K.,Kerwin, S.M.,Robertus, J.D. (deposition date: 2001-05-07, release date: 2002-01-16, Last modification date: 2024-03-13) |
| Primary citation | Miller, D.J.,Ravikumar, K.,Shen, H.,Suh, J.K.,Kerwin, S.M.,Robertus, J.D. Structure-based design and characterization of novel platforms for ricin and shiga toxin inhibition. J.Med.Chem., 45:90-98, 2002 Cited by PubMed Abstract: Ribosome inhibiting proteins, RIPs, are a widespread family of toxic enzymes. Ricin is a plant toxin used as a poison and biological warfare agent; shiga toxin is a homologue expressed by pathogenic strains of E. coli. There is interest in creating effective antidote inhibitors to this class of enzymes. RIPs act by binding and hydrolyzing a specific adenine base from rRNA. Previous virtual screens revealed that pterins could bind in the specificity pocket of ricin and inhibit the enzyme. In this paper we explore a range of compounds that could serve as better platforms for inhibitor design. This establishes the importance of key hydrogen bond donors and acceptors for active-site complementarity. 8-Methyl-9-oxoguanine is a soluble compound that has the best inhibitory properties of any platform tested. The X-ray structure of this complex revealed that the inhibitor binds in an unexpected way that provides insight for future design. Several inhibitors of ricin were also shown to be inhibitors of shiga toxin, suggesting this program has the potential to develop effective antidotes to an important form of food poisoning. PubMed: 11754581DOI: 10.1021/jm010186s PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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