Examination of the Ligand-Binding and Enzymatic Properties of a Bilin-Binding Protein from the Poisonous Caterpillar Lonomia obliqua

@inproceedings{Veiga2014ExaminationOT,
  title={Examination of the Ligand-Binding and Enzymatic Properties of a Bilin-Binding Protein from the Poisonous Caterpillar Lonomia obliqua},
  author={Ana Beatriz Gorini Veiga and Jose M. C. Ribeiro and Ivo M B Francischetti and Xueqing Xu and J. A. Guimar{\~a}es and John F. Andersen},
  booktitle={PloS one},
  year={2014}
}
The bilin-binding proteins (BBP) from lepidopteran insects are members of the lipocalin family of proteins and play a special role in pigmentation through the binding of biliverdin IXγ. Lopap, a BBP-like protein from the venom of the toxic caterpillar Lonomia obliqua has been reported to act as a serine protease that activates the coagulation proenzyme prothrombin. Here we show that BBPLo, a variant of lopap from the same organism binds biliverdin IXγ, forming a complex that is spectrally… CONTINUE READING
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