PH Domain of Serine-Threonine Protein Kinase B (RAC-PKB)

Expression and Binding Assay for Phosphoinositides and Inositol Phosphates
  • Matthias Frech
  • Brian A. Hemmings
Part of the Methods in Molecular Biology™ book series (MIMB, volume 88)


The Pleckstrin homology (PH) domain, as a recent newcomer to the family of protein modules involved in signal transduction, has attracted great interest (1, 2, 3). The PH domain was first recognized as an internal repeat in pleckstrin, the major substrate of protein kinase C in activated platelets (4). Initially overlooked because of the very low sequence similarity between the different PH domains, presently over 90 proteins are known to possess PH domains (5, 6, 7, 8, 9). This domain is often found in proteins involved in signal transduction or cytoskeletal function and forms an independent folding domain of about 100 amino acids. Despite of the very low similarity, their three-dimensional structures are highly related. Several structures of isolated PH domains derived from different proteins are known: pleckstrin (10), dynamin (11, 12, 13, 14), β-spectrin (15, 16, 17), and phospholipaseCδ-1 (18).


Phosphate Group Tryptophan Residue Inositol Phosphate Pleckstrin Homology Pleckstrin Homology Domain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Humana Press Inc. 1998

Authors and Affiliations

  • Matthias Frech
    • 1
  • Brian A. Hemmings
    • 1
  1. 1.Friedrich Miescher InstituteBaselSwitzerland

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