This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1seg
From Proteopedia
m (Protected "1seg" [edit=sysop:move=sysop]) |
Revision as of 08:39, 23 April 2014
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
