Binding of chimeric analogs of Ie[control]-conotoxin MVIIA and MVIIC to the N- and P/Q-type calcium channels
Despite their high sequence homology, the peptide neurotoxins Ie[control]-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 Ie[control]-conotoxin MVIIA and MVIIC were syn...
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Published in | FEBS letters Vol. 414; no. 2; pp. 480 - 484 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
08.09.1997
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Online Access | Get full text |
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Summary: | Despite their high sequence homology, the peptide neurotoxins Ie[control]-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 Ie[control]-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 Ie[control]-conotoxin molecule. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-2 |
ISSN: | 0014-5793 |
DOI: | 10.1016/S0014-5793(97)01056-9 |