1i1e

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Revision as of 14:51, 20 November 2007

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spinqualitylabelsall models 1i1e, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH DOXORUBICIN

Overview

The neurotoxins of Clostridium botulinum and tetanus bind to gangliosides, as a first step of their toxin activity. Identifying suitable receptors, that compete with gangliosides could prevent toxin binding to the neuronal, cells. A possible ganglioside-binding site of the botulinum neurotoxin B, (BoNT/B) has already been proposed and evidence is now presented for a, drug binding to botulinum neurotoxin B from structural studies., Doxorubicin, a well known DNA intercalator, binds to the neurotoxin at the, receptor-binding site proposed earlier. The structure of the, BoNT/B-doxorubicin complex reveals that doxorubicin has interactions with, the neurotoxin similar to those of sialyllactose. The aglycone moiety of, the doxorubicin stacks with tryptophan 1261 and interacts with histidine, 1240 of the binding domain. Here, the possibility is presented of, designing a potential antagonist for these neurotoxins from, crystallographic analysis of the neurotoxin-doxorubicin complex, which, will be an excellent lead compound.

About this Structure

1I1E is a Single protein structure of sequence from Clostridium botulinum with DM2, ZN and SO4 as ligands. Active as Bontoxilysin, with EC number 3.4.24.69 Full crystallographic information is available from OCA.

Reference

Crystallographic evidence for doxorubicin binding to the receptor-binding site in Clostridium botulinum neurotoxin B., Eswaramoorthy S, Kumaran D, Swaminathan S, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1743-6. Epub 2001, Oct 25. PMID:11679763

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