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Origin of Functional Diversities in Taiwan Banded Krait (Bungarus multicinctus) Three-finger Proteins
| Content Provider | Semantic Scholar |
|---|---|
| Author | Chang, Long-Sen Kao, Pei-Hsiu |
| Copyright Year | 2009 |
| Abstract | 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. |
| Starting Page | 57 |
| Ending Page | 64 |
| Page Count | 8 |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/S1877-8607(10)60001-X |
| Volume Number | 1 |
| Alternate Webpage(s) | https://core.ac.uk/download/pdf/82292636.pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/S1877-8607%2810%2960001-X |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
