The PH superfold: a structural scaffold for multiple functions

Trends Biochem Sci. 1999 Nov;24(11):441-5. doi: 10.1016/s0968-0004(99)01472-3.


Pleckstrin homology (PH) domains form a structurally conserved family that is associated with many regulatory pathways within the cell. Domains with a nearly identical fold are found in other families that share no sequence similarity, suggesting the existence of a stable PH superfold. The PH domains generally function as regulated membrane-binding modules that bind to inositol lipids and respond to upstream signals by targeting the host proteins to the correct cellular sites. The other domains with a similar fold, such as the phosphotyrosine binding domains, recognize protein ligands.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Blood Proteins / chemistry*
  • Blood Proteins / metabolism*
  • Enzyme Activation
  • Ligands
  • Phosphatidylinositols / metabolism
  • Phosphoproteins*
  • Protein Conformation
  • Protein Folding*
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid*
  • Static Electricity
  • Structure-Activity Relationship


  • Blood Proteins
  • Ligands
  • Phosphatidylinositols
  • Phosphoproteins
  • platelet protein P47