Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains.

@article{Ferguson2000StructuralBF,
  title={Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains.},
  author={Kathryn M. Ferguson and Jennifer M Kavran and Vijay G Sankaran and Evelyne. Fournier and Steven Jay Isakoff and Edward Y Skolnik and Mark A Lemmon},
  journal={Molecular cell},
  year={2000},
  volume={6 2},
  pages={
          373-84
        }
}
Pleckstrin homology (PH) domains are protein modules of around 120 amino acids found in many proteins involved in cellular signaling. Certain PH domains drive signal-dependent membrane recruitment of their host proteins by binding strongly and specifically to lipid second messengers produced by agonist-stimulated phosphoinositide 3-kinases (PI 3-Ks). We describe X-ray crystal structures of two different PH domains bound to Ins(1,3,4,5)P4, the head group of the major PI 3-K product PtdIns(3,4,5… CONTINUE READING

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