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J. Biol. Chem., Vol. 265, Issue 11, 6025-6029, Apr, 1990
JA Haack, J Rivier, TN Parks, EE Mena, LJ Cruz and BM Olivera
Conantokin-T, a 21-amino acid peptide which induces sleep-like symptoms in
young mice was purified from the venom of the fish-hunting cone snail,
Conus tulipa. The amino acid sequence of the peptide was determined and
verified by chemical synthesis. The peptide has 4 residues of the modified
amino acid, gamma-carboxyglutamate (Gla). The sequence of the peptide is:
Gly-Glu-Gla-Gla-Tyr-Gln-Lys-Met-Leu-Gla-Asn- Leu-Arg-Gla-Ala-Glu-Val-Lys-
Lys-Asn-Ala-NH2. Conantokin-T inhibits N- methyl-D-aspartate (NMDA)
receptor-mediated calcium influx in central nervous system neurons. This
observation suggests that like conantokin- G (a homologous Conus peptide
with recently identified NMDA antagonist activity) conantokin-T has NMDA
antagonist activity. A sequence comparison of conantokins-T and -G
identifies the 4 Gla residues and the N-terminal dipeptide sequence as
potential key elements for the biological activity of this peptide.
Conantokin-T. A gamma-carboxyglutamate containing peptide with N-methyl- d-aspartate antagonist activity
Department of Biology, University of Utah, Salt Lake City 84112.
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P. K. Bandyopadhyay, J. E. Garrett, R. P. Shetty, T. Keate, C. S. Walker, and B. M. Olivera From the Cover: gamma -Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates PNAS, February 5, 2002; 99(3): 1264 - 1269. [Abstract] [Full Text] [PDF]
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