These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A noncompetitive peptide inhibitor of the nicotinic acetylcholine receptor from Conus purpurascens venom.
    Author: Shon KJ, Grilley M, Jacobsen R, Cartier GE, Hopkins C, Gray WR, Watkins M, Hillyard DR, Rivier J, Torres J, Yoshikami D, Olivera BM.
    Journal: Biochemistry; 1997 Aug 05; 36(31):9581-7. PubMed ID: 9236004.
    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).
    [Abstract] [Full Text] [Related] [New Search]