Pleckstrin homology domains: a common fold with diverse functions.
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.
Rebecchi
M J
MJ
Department of Anesthesiology, State University of New York at Stony Brook 11794, USA. rebecchi@epo.hsc.sunysb.edu
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D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry*; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000737:chemistry; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010750:Phosphoproteins; D011505:Protein-Tyrosine Kinases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D020664:Son of Sevenless Proteins; D013049:Spectrin / Q000737:chemistry; D010738:Type C Phospholipases / Q000737:chemistry
D001798:Blood Proteins; D008565:Membrane Proteins; D010750:Phosphoproteins; D011506:Proteins; D020664:Son of Sevenless Proteins; C039077:platelet protein P47; D013049:Spectrin; D011505:Protein-Tyrosine Kinases; D010738:Type C Phospholipases; D020558:GTP Phosphohydrolases; D034281:Dynamins