1yyn

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(New page: 200px<br /><applet load="1yyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yyn, resolution 2.30&Aring;" /> '''A common binding sit...)
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[[Image:1yyn.gif|left|200px]]<br /><applet load="1yyn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1yyn, resolution 2.30&Aring;" />
caption="1yyn, resolution 2.30&Aring;" />
'''A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin'''<br />
'''A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin'''<br />
==Overview==
==Overview==
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Clostridial neurotoxins are comprised of botulinum (BoNT) and tetanus, (TeNT), which share significant structural and functional similarity., Crystal structures of the binding domain of TeNT complexed with, disialyllactose (DiSia) and a tri-peptide Tyr-Glu-Trp (YEW) have been, determined to 2.3 and 2.2 A, respectively. Both DiSia and YEW bind in a, shallow cleft region on the surface of the molecule in the beta-trefoil, domain, interacting with a set of common residues, Asp1147, Asp1214, Asn1216, and Arg1226. DiSia and YEW binding at the same site in tetanus, toxin provides a putative site that could be occupied either by a, ganglioside moiety or a peptide. Soaking experiments with a mixture of YEW, and DiSia show that YEW competes with DiSia, suggesting that YEW can be, used to block ganglioside binding. A comparison with the TeNT binding, domain in complex with small molecules, BoNT/A and /B, provides insight, into the different modes of ganglioside binding.
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Clostridial neurotoxins are comprised of botulinum (BoNT) and tetanus (TeNT), which share significant structural and functional similarity. Crystal structures of the binding domain of TeNT complexed with disialyllactose (DiSia) and a tri-peptide Tyr-Glu-Trp (YEW) have been determined to 2.3 and 2.2 A, respectively. Both DiSia and YEW bind in a shallow cleft region on the surface of the molecule in the beta-trefoil domain, interacting with a set of common residues, Asp1147, Asp1214, Asn1216, and Arg1226. DiSia and YEW binding at the same site in tetanus toxin provides a putative site that could be occupied either by a ganglioside moiety or a peptide. Soaking experiments with a mixture of YEW and DiSia show that YEW competes with DiSia, suggesting that YEW can be used to block ganglioside binding. A comparison with the TeNT binding domain in complex with small molecules, BoNT/A and /B, provides insight into the different modes of ganglioside binding.
==About this Structure==
==About this Structure==
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1YYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Active as [http://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YYN OCA].
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1YYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Active as [http://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYN OCA].
==Reference==
==Reference==
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:08:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:26 2008''

Revision as of 14:10, 21 February 2008


1yyn, resolution 2.30Å

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A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin

Overview

Clostridial neurotoxins are comprised of botulinum (BoNT) and tetanus (TeNT), which share significant structural and functional similarity. Crystal structures of the binding domain of TeNT complexed with disialyllactose (DiSia) and a tri-peptide Tyr-Glu-Trp (YEW) have been determined to 2.3 and 2.2 A, respectively. Both DiSia and YEW bind in a shallow cleft region on the surface of the molecule in the beta-trefoil domain, interacting with a set of common residues, Asp1147, Asp1214, Asn1216, and Arg1226. DiSia and YEW binding at the same site in tetanus toxin provides a putative site that could be occupied either by a ganglioside moiety or a peptide. Soaking experiments with a mixture of YEW and DiSia show that YEW competes with DiSia, suggesting that YEW can be used to block ganglioside binding. A comparison with the TeNT binding domain in complex with small molecules, BoNT/A and /B, provides insight into the different modes of ganglioside binding.

About this Structure

1YYN is a Single protein structure of sequence from Clostridium tetani. Active as Tentoxilysin, with EC number 3.4.24.68 Full crystallographic information is available from OCA.

Reference

Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin., Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S, Proteins. 2005 Nov 1;61(2):288-95. PMID:16104015

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