1fv2: Difference between revisions

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New page: left|200px<br /><applet load="1fv2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fv2, resolution 2.5Å" /> '''THE HC FRAGMENT OF TE...
 
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[[Image:1fv2.gif|left|200px]]<br /><applet load="1fv2" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fv2.gif|left|200px]]<br /><applet load="1fv2" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fv2, resolution 2.5&Aring;" />
caption="1fv2, resolution 2.5&Aring;" />
'''THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH AN ANALOGUE OF ITS GANGLIOSIDE RECEPTOR GT1B'''<br />
'''THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH AN ANALOGUE OF ITS GANGLIOSIDE RECEPTOR GT1B'''<br />


==Overview==
==Overview==
Tetanus toxin, a member of the family of Clostridial neurotoxins, is one, of the most potent toxins known. The crystal structure of the complex of, the COOH-terminal fragment of the heavy chain with an analogue of its, ganglioside receptor, GT1b, provides the first direct identification and, characterization of the ganglioside-binding sites. The ganglioside induces, cross-linking by binding to two distinct sites on the Hc molecule. The, structure sheds new light on the binding of Clostridial neurotoxins to, receptors on neuronal cells and provides important information relevant to, the design of anti-tetanus and anti-botulism therapeutic agents.
Tetanus toxin, a member of the family of Clostridial neurotoxins, is one of the most potent toxins known. The crystal structure of the complex of the COOH-terminal fragment of the heavy chain with an analogue of its ganglioside receptor, GT1b, provides the first direct identification and characterization of the ganglioside-binding sites. The ganglioside induces cross-linking by binding to two distinct sites on the Hc molecule. The structure sheds new light on the binding of Clostridial neurotoxins to receptors on neuronal cells and provides important information relevant to the design of anti-tetanus and anti-botulism therapeutic agents.


==About this Structure==
==About this Structure==
1FV2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani] with PO4 and CEQ as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1FV2 OCA].  
1FV2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=CEQ:'>CEQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1FV2 OCA].  


==Reference==
==Reference==
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[[Category: Black, I.]]
[[Category: Black, I.]]
[[Category: Emsley, P.]]
[[Category: Emsley, P.]]
[[Category: Fairweather, N.F.]]
[[Category: Fairweather, N F.]]
[[Category: Fotinou, C.]]
[[Category: Fotinou, C.]]
[[Category: Isaacs, N.W.]]
[[Category: Isaacs, N W.]]
[[Category: Ishida, H.]]
[[Category: Ishida, H.]]
[[Category: Kiso, M.]]
[[Category: Kiso, M.]]
[[Category: Sinha, K.A.]]
[[Category: Sinha, K A.]]
[[Category: CEQ]]
[[Category: CEQ]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: toxin]]
[[Category: toxin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:19:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:55 2008''

Revision as of 13:42, 21 February 2008

File:1fv2.gif


1fv2, resolution 2.5Å

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THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH AN ANALOGUE OF ITS GANGLIOSIDE RECEPTOR GT1B

OverviewOverview

Tetanus toxin, a member of the family of Clostridial neurotoxins, is one of the most potent toxins known. The crystal structure of the complex of the COOH-terminal fragment of the heavy chain with an analogue of its ganglioside receptor, GT1b, provides the first direct identification and characterization of the ganglioside-binding sites. The ganglioside induces cross-linking by binding to two distinct sites on the Hc molecule. The structure sheds new light on the binding of Clostridial neurotoxins to receptors on neuronal cells and provides important information relevant to the design of anti-tetanus and anti-botulism therapeutic agents.

About this StructureAbout this Structure

1FV2 is a Single protein structure of sequence from Clostridium tetani with and as ligands. Active as Tentoxilysin, with EC number 3.4.24.68 Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin., Fotinou C, Emsley P, Black I, Ando H, Ishida H, Kiso M, Sinha KA, Fairweather NF, Isaacs NW, J Biol Chem. 2001 Aug 24;276(34):32274-81. Epub 2001 Jun 19. PMID:11418600

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