Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha.

@article{Stahelin2006StructuralAM,
  title={Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha.},
  author={Robert V. Stahelin and Dimitrios Karathanassis and Karol S. Bruzik and Michael D. Waterfield and Jer{\'o}nimo Bravo and Roger L Williams and Wonhwa Cho},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 51},
  pages={39396-406}
}
Phox homology (PX) domains, which have been identified in a variety of proteins involved in cell signaling and membrane trafficking, have been shown to interact with phosphoinositides (PIs) with different affinities and specificities. To elucidate the structural origin of diverse PI specificities of PX domains, we determined the crystal structure of the PX domain from phosphoinositide 3-kinase C2alpha (PI3K-C2alpha), which binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)). To… CONTINUE READING

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