Binding of a Pleckstrin homology domain protein to phosphoinositide in membranes: a miniaturized FRET-based assay for drug screening.

@article{Hamman2002BindingOA,
  title={Binding of a Pleckstrin homology domain protein to phosphoinositide in membranes: a miniaturized FRET-based assay for drug screening.},
  author={Brian Hamman and Brian A. Pollok and Todd Bennett and Janet Allen and Roger Heim},
  journal={Journal of biomolecular screening},
  year={2002},
  volume={7 1},
  pages={45-55}
}
Pleckstrin homology (PH) domains are present in key proteins involved in many vital cell processes. For example, the PH domain of Bruton's tyrosine kinase (Btk) binds to phosphatidylinositol triphosphate (PIP(3)) in the plasma membrane after stimulation of the B-cell receptor in B cells. Mutations in the Btk PH domain result in changes in its affinity for PIP(3), with higher binding leading to cell transformation in vitro and lower binding leading to antibody deficiencies in both humans and… CONTINUE READING