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Comparative pharmacology and cloning of two novel arachnid sodium channels: Exploring the adaptive insensitivity of scorpion to its toxins
Author(s) -
Zuo Xiao-Pan,
He Hui-Qiong,
He Ming,
Liu Zhi-Rui,
Xu Qing,
Ye Jian-Guo,
Ji Yong-Hua
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.024
Subject(s) - scorpion , sodium channel , scorpion toxin , amino acid , scorpion venoms , chemistry , sodium , venom , spider toxin , complementary dna , biology , biochemistry , receptor , gene , glutamate receptor , organic chemistry
Scorpion toxins have been found lacking effect on Na + current of its own sodium channel, whereas the molecular mechanism remains mystery. In this study, the binding affinity of pharmacologically distinct scorpion toxins was found much weaker to scorpion ( Buthus martensii ) nerve synaptosomes than to spider ( Ornithoctonus huwena ) ones. The sodium channel cDNA from these two species were further cloned. The deduced proteins contain 1871 and 1987 amino acids respectively. Several key amino acid substitutions, i.e., A1610V, I1611L and S1617K, are found in IVS3–S4 constituting receptor site‐3, and for receptor site‐4, two residues (Leu‐Pro) are inserted near IIS4 of scorpion sodium channel.