1i1e

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(New page: 200px<br /><applet load="1i1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1e, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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'''CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH DOXORUBICIN'''<br />
'''CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH DOXORUBICIN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1I1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with DM2, ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I1E OCA].
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1I1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with <scene name='pdbligand=DM2:'>DM2</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1E OCA].
==Reference==
==Reference==
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[[Category: neurotoxin]]
[[Category: neurotoxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:58:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:01 2008''

Revision as of 11:07, 21 February 2008


1i1e, resolution 2.5Å

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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 , and 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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