| Literature DB >> 9236004 |
K J Shon1, M Grilley, R Jacobsen, G E Cartier, C Hopkins, W R Gray, M Watkins, D R Hillyard, J Rivier, J Torres, D Yoshikami, B M Olivera.
Abstract
A paralytic peptide, psi-conotoxin Piiie has been purified and characterized from Conus purpurascens venom. Electrophysiological studies indicate that the peptide inhibits the nicotinic acetylcholine receptor (nAChR). However, the peptide does not block the binding of alpha-bungarotoxin, a competitive nAChR antagonist. Thus, psi-conotoxin Piiie appears to inhibit the receptor at a site other than the acetylcholine-binding site. As ascertained by sequence analysis, mass spectrometry, and chemical synthesis, the peptide has the following covalent structure: HOOCCLYGKCRRYOGCSSASCCQR* (O = 4-trans hydroxyproline; * indicates an amidated C-terminus). The disulfide connectivity of the toxin is unrelated to the alpha- or the alphaA-conotoxins, the Conus peptide families that are competitive inhibitors of the nAChR, but shows homology to the mu-conotoxins (which are Na+ channel blockers).Entities:
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Year: 1997 PMID： 9236004 DOI： 10.1021/bi970235w
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162