1il3: Difference between revisions

Revision as of 13:26, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1il3.png

Template:STRUCTURE 1il3

STRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 7-DEAZAGUANINESTRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 7-DEAZAGUANINE

Template:ABSTRACT PUBMED 11754581

About this StructureAbout this Structure

1IL3 is a Single protein structure of sequence from Ricinus communis. Full crystallographic information is available from OCA.

ReferenceReference

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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-'''STRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 7-DEAZAGUANINE'''
+===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.
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 [[Category: Structure-based design]]
 [[Category: Toxin-inhibitor complex]]
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