Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity.

@article{Zheng1996IdentificationOT,
  title={Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity.},
  author={Jiangjun Zheng and Sean M. Cahill and Mark A Lemmon and David Fushman and Joseph Schlessinger and David Cowburn},
  journal={Journal of molecular biology},
  year={1996},
  volume={255 1},
  pages={14-21}
}
It has recently been suggested that pleckstrin homology (PH) domains bind specifically to phospholipids, with phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) being most strongly bound. This observation suggests that PH domains may be responsible for membrane association of proteins in which they occur. Further, this membrane association may be regulated by enzymes that modify lipid head groups to which PH domains may bind. We have studied the binding of phospholipids to the PH domain of… CONTINUE READING
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