Pleckstrin homology domains: a common fold with diverse functions

Annu Rev Biophys Biomol Struct. 1998;27:503-28. doi: 10.1146/annurev.biophys.27.1.503.

Abstract

Pleckstrin homology (PH) motifs are approximately 100 amino-acid residues long and have been identified in nearly 100 different eukaryotic proteins, many of which participate in cell signaling and cytoskeletal regulation. Despite minimal sequence homology, the three-dimensional structures are remarkably conserved. This review gives an overview of the PH domain architecture and examines the best-studied examples in an attempt to understand their function.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blood Proteins / chemistry*
  • Dynamins
  • GTP Phosphohydrolases / chemistry
  • Humans
  • Membrane Proteins / chemistry
  • Molecular Sequence Data
  • Phosphoproteins*
  • Protein-Tyrosine Kinases / chemistry
  • Proteins / chemistry*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Son of Sevenless Proteins
  • Spectrin / chemistry
  • Type C Phospholipases / chemistry

Substances

  • Blood Proteins
  • Membrane Proteins
  • Phosphoproteins
  • Proteins
  • Son of Sevenless Proteins
  • platelet protein P47
  • Spectrin
  • Protein-Tyrosine Kinases
  • Type C Phospholipases
  • GTP Phosphohydrolases
  • Dynamins