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1seg

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[[Image:1seg.png|left|200px]]
 
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{{STRUCTURE_1seg| PDB=1seg | SCENE= }}
{{STRUCTURE_1seg| PDB=1seg | SCENE= }}
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===Crystal structure of a toxin chimera between Lqh-alpha-IT from the scorpion Leiurus quinquestriatus hebraeus and AAH2 from Androctonus australis hector===
===Crystal structure of a toxin chimera between Lqh-alpha-IT from the scorpion Leiurus quinquestriatus hebraeus and AAH2 from Androctonus australis hector===
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{{ABSTRACT_PUBMED_15133045}}
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==Function==
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[[http://www.uniprot.org/uniprot/SCX2_ANDAU SCX2_ANDAU]] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals.
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{{ABSTRACT_PUBMED_15133045}}
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==About this Structure==
==About this Structure==
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1SEG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Androctonus_australis_hector Androctonus australis hector]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SEG OCA].
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[[1seg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Androctonus_australis_hector Androctonus australis hector]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SEG OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:15133045</ref><references group="xtra"/>
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<ref group="xtra">PMID:015133045</ref><references group="xtra"/><references/>
[[Category: Androctonus australis hector]]
[[Category: Androctonus australis hector]]
[[Category: Cohen, L.]]
[[Category: Cohen, L.]]
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[[Category: Scorpion]]
[[Category: Scorpion]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:46:05 2009''
 

Revision as of 08:39, 23 April 2014

Template:STRUCTURE 1seg

Contents

Crystal structure of a toxin chimera between Lqh-alpha-IT from the scorpion Leiurus quinquestriatus hebraeus and AAH2 from Androctonus australis hector

Template:ABSTRACT PUBMED 15133045

Function

[SCX2_ANDAU] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals.

About this Structure

1seg is a 1 chain structure with sequence from Androctonus australis hector. Full crystallographic information is available from OCA.

Reference

  • Karbat I, Frolow F, Froy O, Gilles N, Cohen L, Turkov M, Gordon D, Gurevitz M. Molecular basis of the high insecticidal potency of scorpion alpha-toxins. J Biol Chem. 2004 Jul 23;279(30):31679-86. Epub 2004 May 8. PMID:15133045 doi:10.1074/jbc.M402048200

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