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FEBS Lett. 2007 Nov 27;581(28):5485-92. Epub 2007 Nov 6.

Mutations in DIIS5 and the DIIS4-S5 linker of Drosophila melanogaster sodium channel define binding domains for pyrethroids and DDT.

Author information

1
School of Biology, The University of Nottingham, University Park, Nottingham, UK. peter.usherwood@nottingham.ac.uk

Abstract

Mutations in the DIIS4-S5 linker and DIIS5 have identified hotspots of pyrethroid and DDT interaction with the Drosophila para sodium channel. Wild-type and mutant channels were expressed in Xenopus oocytes and subjected to voltage-clamp analysis. Substitutions L914I, M918T, L925I, T929I and C933A decreased deltamethrin potency, M918T, L925I and T929I decreased permethrin potency and T929I, L925I and I936V decreased fenfluthrin potency. DDT potency was unaffected by M918T, but abolished by T929I and reduced by L925I, L932F and I936V, suggesting that DIIS5 contains at least part of the DDT binding domain. The data support a computer model of pyrethroid and DDT binding.

PMID:
17991435
DOI:
10.1016/j.febslet.2007.10.057
[Indexed for MEDLINE]
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