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Volume 1, Issue 2, Pages 57-64 (November 2009)

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Origin of Functional Diversities in Taiwan Banded Krait (Bungarus multicinctus) Three-finger Proteins

Long-Sen ChangCorresponding Author Informationemail address, Pei-Hsiu Kao

Received 5 September 2009; received in revised form 3 October 2009; accepted 7 October 2009.

Taiwan banded krait (Bungarus multicinctus) neurotoxins and neurotoxin homologues, including α-bungarotoxin (Bgt), κ-Bgt, γ-Bgt, BM8, BM10-1, BM10-2 and BM14, have been reported. These proteins have a common three-finger scaffold and conserved cysteine residues at homologous positions. Nevertheless, these proteins show functional diversity and sequence variations in loop regions. The genomic DNAs encoding the precursors of α-Bgt, κ-Bgt, γ-Bgt, BM10-1 and BM14 are organized with three exons and two introns. The intron regions of these genes have a high degree of sequence identity, but the protein-coding regions are highly variable with the exception of the signal peptide region. These findings suggest that B. multicinctus three-finger proteins share a common evolutionary origin, and the evolution of snake venom proteins shows a tendency to diversify their functions, which may be beneficial for catching prey. Given that a multitude of functional diversities is noted with three-finger toxins, protein engineering in highly variable regions without distorting the three-finger scaffold may result in the development biopharmaceutical agents with novel functions of scientific and therapeutic interest.

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Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung, Taiwan

Corresponding Author InformationCorresponding author. Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan

PII: S1877-8607(10)60001-X

doi:10.1016/S1877-8607(10)60001-X

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