1il3
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(New page: 200px<br /><applet load="1il3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1il3, resolution 2.8Å" /> '''STRUCTURE OF RICIN A ...)
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Revision as of 15:21, 20 November 2007
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STRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 7-DEAZAGUANINE
Overview
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.
About this Structure
1IL3 is a Single protein structure of sequence from Ricinus communis with 7DG as ligand. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.
Reference
Structure-based design and characterization of novel platforms for ricin and shiga toxin inhibition., Miller DJ, Ravikumar K, Shen H, Suh JK, Kerwin SM, Robertus JD, J Med Chem. 2002 Jan 3;45(1):90-8. PMID:11754581
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