Chinese Journal of Natural Medicines (中国天然药物) 2009/7:2 PP.145-149
AIM: To illustrate the structure and function of five hematoxin sequences reported in four jellyfish and explore the possible mechanism of pathogenesis. METHODS: Bioinformatic methods were used to analyze the composition and sequence of amino acid residues, physico-chemical property, signal peptide, membrane spanning domain, hydrophobicity or hydrophilicity, secondary structure, conserved region and molecular phylogenetic evolution. RESULT and CONCLUSIONS: The results showed that the five jellyfish hematoxins were similar in composition and sequence of amino acid residues and physico-chemical property. The amino acid sequences of jellyfish hematoxins contained membrane spanning domain and hydrophobic regions; with a possible cleavage site in the signal peptide between the amino acid residues 20 and 21; α-helix and random coil were the major motifs of predicted secon-dary structure while β-turn and extended strand spread in the whole protein; There were four conserved amino acid sequences in three of the five hematoxins and similar phylogenetic trees were constructed by both NJ and MP methods.
Funds：This project was supported by the Natural Science Foundation of Shanghai Municipal Government (No. 06ZR14111) and “Eleventh Five-Year Plan” for Medical Science Development of PLA (No. 06Z020).
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