Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of signalling proteins, where they serve as simple targeting domains that bind lipids [1, 2, 3].

PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1), Shc adaptor and Numb; to the Ran-binding domain, found in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain), found in Enabled, VASP (vasodilator-stimulated phosphoprotein), Homer and WASP actin regulatory protein; to the third domain of FERM, found in moesin, radixin, ezrin, merlin and talin; and to the PH-like domain of neurobeachin.

This entry recognises PH domains and other structurally related domains.

1. Membrane targeting by pleckstrin homology domains. Curr. Top. Microbiol. Immunol. 282, 49-88
2. Phosphoinositide recognition domains. Traffic 4, 201-13
3. A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol. Syst. Biol. 6, 430

Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of sign
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