Precursors of three unique cysteine-rich peptides from the scorpion Buthus martensii Karsch.

Scorpion venoms contain a large number of small peptides with diverse primary structures and unique pharmacological functions. From a cDNA library prepared from venom glands of the Chinese scorpion Buthus martensii Karsch, clones encoding precursors of three unique cysteine-rich peptides named BmTXKS3, BmTXLP2 and BmAP1 have been isolated and sequenced. These precursors are composed of 54, 94 and 89 amino acids, respectively, containing a signal peptide in their N-termini. Sequence analysis shows that BmTXKS3 and BmTXLP2 are two novel members of a scorpion toxin family sharing cysteine-stabilized alpha-helical folds. BmAP1 possesses a distinctive cystine framework, which is similar to some serine protease inhibitors and the segments of several extracellular proteins.