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

Kazuki Sato 1 Cécile Raymond 2 Nicole Martin-Moutot 2 Toru Sasaki 1 Akira Omori 1 Atsuko Ohtake 1 Jae Il Kim 1 Toshiyuki Kohno 1 Masami Takahashi 1 Michael Seagar 2
1 MKILS - Mitsubishi Kasei Institute of Life Sciences [Tokyo, Japon]
2 Inserm U374 - Faculté de Médecine - secteur Nord Marseille - Neurobiologie des Canaux Ioniques
Abstract : 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.
Keywords : w-Conotoxin MVIIA w-Conotoxin MVIIC Calcium channel Chimeric analog
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https://www.hal.inserm.fr/inserm-03246882
Contributor : Cécile Raymond <>
Submitted on : Wednesday, June 2, 2021 - 4:23:04 PM
Last modification on : Wednesday, June 2, 2021 - 4:55:03 PM

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Kazuki Sato, Cécile Raymond, Nicole Martin-Moutot, Toru Sasaki, Akira Omori, et al.. Binding of chimeric analogs of w-conotoxin MVIIA and MVIIC to the N-and P/Q-type calcium channels. FEBS Letters, Wiley, 1997, 414 (2), pp.480-4. ⟨10.1016/s0014-5793(97)01056-9⟩. ⟨inserm-03246882⟩

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