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Binding of chimeric analogs of ω‐conotoxin MVIIA and MVIIC to the N‐ and P/Q‐type calcium channels
Author(s) -
Kazuki Sato,
Cécile Raymond,
Nicole Martin-Moutôt,
Toru Sasaki,
Akira Omori,
Atsuko Ohtake,
Jae Il Kim,
Toshiyuki Kohno,
Masami Takahashi,
Michael Seagar
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01056-9
Subject(s) - conotoxin , calcium channel , chemistry , n type calcium channel , peptide , calcium , voltage dependent calcium channel , peptide sequence , amino acid , stereochemistry , t type calcium channel , biochemistry , gene , organic chemistry
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.