PH domain

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A Pleckstrin Homology domain or PH Domain is a protein composed of around 100 amino acids that is found within numerous protein families involved with intracellular signalling[1]. Originally found in Pleckstrin [2] it has since been detected in around 200 human proteins[3] as well as other eukaryotic proteins. The primary function of the domain appears to be the binding of inositol phosphates though other related proteins are also able to bind. The structure though varying to some degree depending on which domains the PH domain is within, certain features are conserved. These are the presence of a C-terminal alpha helix closely associated with a beta sheet consisting of 7 strands.[4]
  1. Mussacchio A, Gibson T, Rice P, Thompson J, Saraste M. 1993 The PH Domain: a Common Piece in the Structural Patchwork of Siganlling Proteins. Trends in Biochemical Sciences [e-journal] 18(9): 343-8
  2. Mayer B.J, Ren R., Clark K.L., Baltimore D., 1993 A Putative Modular Domain Present in Diverse Signalling Proteins. Cell [e-journal] 73(4): 629-630
  3. Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P, 2008. Molecular Biology of the Cell, 5th Edition. New York: Garland Science. p933
  4. Saraste M, Hyvönen M, 1995. Pleckstrin homology domains: a fact file. Current Opinions in Structural Biology, [e-journal] 5(3): 403-8.
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