Binding of chimeric analogs of w-conotoxin MVIIA and MVIIC to the N-and P/Q-type calcium channels

Despite their high sequence homology, the peptide neurotoxins ¢o-conotoxin MVIIA and MVIIC selectively block N-and P/Q-type calcium channels, respectively. To study the recognition mechanism of calcium channel subtypes, two chimeric analogs of ¢o-conotoxin MVIIA and MVIIC were synthesized by exchang...

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Bibliographic Details
Published in:FEBS letters 1997-09, Vol.414 (2), p.480-4
Main Authors: Sato, Kazuki, Raymond, Cécile, Martin-Moutot, Nicole, Sasaki, Toru, Omori, Akira, Ohtake, Atsuko, Il Kim, Jae, Kohno, Toshiyuki, Takahashi, Masami, Seagar, Michael
Format: Article
Language:English
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Life Sciences
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Summary:Despite their high sequence homology, the peptide neurotoxins ¢o-conotoxin MVIIA and MVIIC selectively block N-and P/Q-type calcium channels, respectively. To study the recognition mechanism of calcium channel subtypes, two chimeric analogs of ¢o-conotoxin MVIIA and MVIIC were synthesized by exchanging their N-and C-terminal halves. Binding assay for both N-and P/Q-type calcium channels showed that amino acid residues restricted to the N-terminal half are important for the recognition of N-type channels, whereas essential residues for P/Q-type channel recognition are widely spread over the whole ¢o-conotoxin molecule.
ISSN:0014-5793
1873-3468
DOI:10.1016/s0014-5793(97)01056-9