Pleckstrin homology (PH) like domains - versatile modules in protein-protein interaction platforms

FEBS Lett. 2012 Aug 14;586(17):2662-73. doi: 10.1016/j.febslet.2012.06.006. Epub 2012 Jun 19.


The initial reports on pleckstrin homology (PH) domains almost 20 years ago described them as sequence feature of proteins involved in signal transduction processes. Investigated at first along the phospholipid binding properties of a small subset of PH representatives, the PH fold turned out to appear as mediator of phosphotyrosine and polyproline peptide binding to other signaling proteins. While phospholipid binding now seems rather the exception among PH-like domains, protein-protein interactions established as more and more important feature of these modules. In this review we focus on the PH superfold as a versatile protein-protein interaction platform and its three-dimensional integration in an increasing number of available multidomain structures.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Blood Proteins / chemistry*
  • Crystallography, X-Ray / methods
  • GTP-Binding Proteins / chemistry
  • Guanosine Triphosphate / chemistry
  • Humans
  • Ligands
  • Models, Molecular
  • Peptides / chemistry
  • Phospholipids / chemistry
  • Phosphoproteins / chemistry*
  • Protein Conformation
  • Protein Folding
  • Protein Interaction Mapping / methods*
  • Protein Structure, Tertiary*
  • Signal Transduction


  • Blood Proteins
  • Ligands
  • Peptides
  • Phospholipids
  • Phosphoproteins
  • platelet protein P47
  • Guanosine Triphosphate
  • GTP-Binding Proteins