Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.

@article{Jia2016StructuralBF,
  title={Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.},
  author={Ning Jia and Nan Liu and Wang Cheng and Yong-liang Jiang and Hui Sun and Lan-lan Chen and Junhui Peng and Yonghui Zhang and Yue-He Ding and Zhi-Hui Zhang and Xuejuan Wang and Gang Cai and Junfeng Wang and Meng-Qiu Dong and Zhiyong Zhang and Hui Wu and Hong-Wei Wang and Yuxing Chen and Cong-Zhao Zhou},
  journal={EMBO reports},
  year={2016},
  volume={17 2},
  pages={235-48}
}
Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a β-prism lectin module followed by an aerolysin module. Specific binding of the… CONTINUE READING
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