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Media type:
E-Article
Title:
The μO‐conotoxin MrVIA inhibits voltage‐gated sodium channels by associating with domain‐3
Contributor:
Zorn, Stefan;
Leipold, Enrico;
Hansel, Alfred;
Bulaj, Grzegorz;
Olivera, Baldomero M.;
Terlau, Heinrich;
Heinemann, Stefan H.
Published:
Wiley, 2006
Published in:
FEBS Letters, 580 (2006) 5, Seite 1360-1364
Language:
English
DOI:
10.1016/j.febslet.2006.01.057
ISSN:
0014-5793;
1873-3468
Origination:
Footnote:
Description:
Several families of peptide toxins from cone snails affect voltage‐gated sodium (NaV) channels: μ‐conotoxins block the pore, δ‐conotoxins inhibit channel inactivation, and μO‐conotoxins inhibit NaV channels by an unknown mechanism. The only currently known μO‐conotoxins MrVIA and MrVIB from Conus marmoreus were applied to cloned rat skeletal muscle (NaV1.4) and brain (NaV1.2) sodium channels in mammalian cells. A systematic domain‐swapping strategy identified the C‐terminal pore loop of domain‐3 as the major determinant for NaV1.4 being more potently blocked than NaV1.2 channels. μO‐conotoxins therefore show an interaction pattern with NaV channels that is clearly different from the related μ‐ and δ‐conotoxins, indicative of a distinct molecular mechanism of channel inhibition.