ABSTRACT
Conantokin is a distinct family of conotoxin superfamily. Its members share considerable overall sequence homology. Their defining attributes include a high relative content of gamma-carboxyglutamic acid (Gla). They are generally devoid of disufide-loop contrasted with other conotoxins (except for conantokin-R). Upon binding to metal ions, the content of alpha-helix conformation increases in different degrees. They inhibit NMDA (N-methyl-D-aspartate) receptors; moreover, different conantokin species present different NMDA receptor subunit specificity. It can induce sleep-like symptoms in young mice when delivered intracranially. Analysis of sequences and structures indicates that the high conserved residues of these peptides are determinative in their structures and functions. In this article, the relationships of their structures and functions are reviewed in detail.