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  The μO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3

Zorn, S., Leipold, E., Hansel, A., Bulaj, G., Olivera, B. M., Terlau, H., et al. (2006). The μO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3. FEBS Letters, 580(5), 1360-1364.

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 Creators:
Zorn, Stefan, Author
Leipold, Enrico, Author
Hansel, Alfred, Author
Bulaj, Gregorz, Author
Olivera, Baldomero M., Author
Terlau, Heinrich1, Author              
Heinermann, Stefan H., Author
Affiliations:
1Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173655              

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Free keywords: sodium channel; conotoxin; neurotoxin; patch clamp; channel block; pain MOLECULAR-MECHANISMS; EXPRESSION; CURRENTS; NEURONS; TOXINS
 Abstract: Several families of peptide toxins from cone snails affect voltage-gated sodium (Na-V) channels: mu-conotoxins block the pore, delta-conotoxins inhibit channel inactivation, and mu O-conotoxins inhibit Na-V channels by an unknown mechanism. The only currently known mu O-conotoxins MrVIA and MrVIB from Conus marmoreus were applied to cloned rat skeletal muscle (Na(V)1.4) and brain (Na(V)1.2) sodium channels in mammalian cells. A systematic domain-swapping strategy identified the C-terminal pore loop of domain-3 as the major determinant for Na(V)1.4 being more potently blocked than Na(V)1.2 channels. mu O-conotoxins therefore show an interaction pattern with Na-V channels that is clearly different from the related mu- and delta-conotoxins, indicative of a distinct molecular mechanism of channel inhibition. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2006-02
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 292204
ISI: 000235597700026
ISI: 000235597700026
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Title: FEBS Letters
  Alternative Title : Febs Lett.
Source Genre: Journal
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Pages: - Volume / Issue: 580 (5) Sequence Number: - Start / End Page: 1360 - 1364 Identifier: ISSN: 0014-5793