Structure of the PX domain of SNX25 reveals a novel phospholipid recognition model by dimerization in the PX domain.

@article{Su2017StructureOT,
  title={Structure of the PX domain of SNX25 reveals a novel phospholipid recognition model by dimerization in the PX domain.},
  author={Kai Su and Tingting Xu and Zhijun Yu and Jiabin Zhu and Yulong Zhang and Minhao Wu and Ying Xiong and Jinsong Liu and Jinxin Xu},
  journal={FEBS letters},
  year={2017},
  volume={591 13},
  pages={2011-2018}
}
SNX25, a regulator of GPCR signaling-phox-homology (PX) domain containing sorting nexin (SNX) member, has been proposed to be involved in the lysosomal degradation of the transforming growth factor β receptor and the development of temporal lobe epilepsy. Targeting to the endosomal membranes by the specific binding of phosphorylated phosphatidylinositols… CONTINUE READING