| Autor: |
Sato, Kazuki, Raymond, Cecile, Martin-Moutot, Nicole, Sasaki, Toru, Omori, Akira, Ohtake, Atsuko, Kim, Jae Il, Kohno, Toshiyuki, Takahashi, Masami, Seagar, Michael |
| Zdroj: |
FEBS Letters; September 1997, Vol. 414 Issue: 2 p480-484, 5p |
| Abstrakt: |
Despite their high sequence homology, the peptide neurotoxins ω-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 ω-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 ω-conotoxin molecule. |
| Databáze: |
Supplemental Index |
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