4hhf
From Proteopedia
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[[Category: Durek, T.]] | [[Category: Durek, T.]] | ||
Revision as of 15:16, 19 February 2014
Contents |
Crystal Structure of chemically synthesized scorpion alpha-toxin OD1
Template:ABSTRACT PUBMED 23527544
Function
[SCX1_ODODO] Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Mammalian sodium channels Nav1.5/SCN2A (only at micromolar concentrations), Nav1.7/SCN9A (EC(50)=4.5 nM) and insect sodium channel para/tipE (EC(50)=80 nM) are affected by this toxin, whereas mammalian sodium channels Nav1.2/SCN2A, Nav1.3/SCN3A, and Nav1.8/SCN10A are unaffected by high concentrations.[1] [2]
About this Structure
4hhf is a 1 chain structure. Full crystallographic information is available from OCA.
Reference
- Durek T, Vetter I, Wang CI, Motin L, Knapp O, Adams DJ, Lewis RJ, Alewood PF. Chemical Engineering and Structural and Pharmacological Characterization of the alpha-Scorpion Toxin OD1. ACS Chem Biol. 2013 Apr 3. PMID:23527544 doi:http://dx.doi.org/10.1021/cb400012k
- ↑ Jalali A, Bosmans F, Amininasab M, Clynen E, Cuypers E, Zaremirakabadi A, Sarbolouki MN, Schoofs L, Vatanpour H, Tytgat J. OD1, the first toxin isolated from the venom of the scorpion Odonthobuthus doriae active on voltage-gated Na+ channels. FEBS Lett. 2005 Aug 1;579(19):4181-6. PMID:16038905 doi:S0014-5793(05)00797-0
- ↑ Maertens C, Cuypers E, Amininasab M, Jalali A, Vatanpour H, Tytgat J. Potent modulation of the voltage-gated sodium channel Nav1.7 by OD1, a toxin from the scorpion Odonthobuthus doriae. Mol Pharmacol. 2006 Jul;70(1):405-14. Epub 2006 Apr 26. PMID:16641312 doi:mol.106.022970
