1seg
From Proteopedia
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
Categories: Androctonus australis hector | Cohen, L. | Frolow, F. | Froy, O. | Gilles, N. | Gordon, D. | Gurevitz, M. | Karbat, I. | Turkov, M. | Chimera | Scorpion | Toxin