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Molecular cloning and sequencing of two ‘short chain’ and two ‘long chain’ K + channel‐blocking peptides from the Chinese scorpion Buthus martensii Karsch
Author(s) -
Zhu Shunyi,
Li Wenxin,
Zeng Xianchun,
Jiang Dahe,
Mao Xin,
Liu Hui
Publication year - 1999
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/s0014-5793(99)01101-1
Subject(s) - scorpion , scorpion venoms , peptide , complementary dna , scorpion toxin , chemistry , peptide sequence , venom , structural similarity , biology , gene , microbiology and biotechnology , biochemistry
Five full‐length cDNAs encoding the precursors of two ‘short chain’ scorpion non‐toxic peptides active on Ca 2+ ‐activated K + channels (BmP02 and BmP03) and two novel putative long chain K + channel‐blocking peptides (named BmTXKβ and BmTXKβ2) were first isolated from the venom gland cDNA library of the Chinese scorpion Buthus martensii Karsch (BmK). BmTXKβ2 showed a high similarity with AaTXKβ, while BmTXKβ was completely different in the deduced primary structure from the long chain and short chain scorpion toxins already characterized. Thus, BmTXKβ expands the scorpion long chain K + channel‐blocking peptide family. Although little sequence similarity exists between the above two short and two long peptides, they are similar at the positions of six cysteines, suggesting that they should all share a similar scaffold composed of an α‐helix and a three‐stranded β‐sheet.