Solution structure of BmP02, a new potassium channel blocker from the venom of the Chinese scorpion Buthus martensi Karsch.

@article{Xu2000SolutionSO,
  title={Solution structure of BmP02, a new potassium channel blocker from the venom of the Chinese scorpion Buthus martensi Karsch.},
  author={Yingqi Xu and J Wu and Jianjun Pei and Yunyu Shi and Yingchun Ji and Qiqing Tong},
  journal={Biochemistry},
  year={2000},
  volume={39 45},
  pages={
          13669-75
        }
}
BmP02 is a 28-amino acid residue peptide purified from the venom of the Chinese scorpion Buthus martensi Karsch, which had been demonstrated to be a weak blocker of apamin-sensitive calcium-activated potassium channels. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmP02. The results show that BmP02 formed a alpha/beta scorpion fold, the typical three-dimensional structure adopted by most short chain scorpion toxins whose structures have been… CONTINUE READING

Topics from this paper.

Citations

Publications citing this paper.