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
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Blood Proteins / chemistry*
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Dynamins
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GTP Phosphohydrolases / chemistry
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Humans
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Membrane Proteins / chemistry
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Molecular Sequence Data
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Phosphoproteins*
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Protein-Tyrosine Kinases / chemistry
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Proteins / chemistry*
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Sequence Alignment
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Sequence Homology, Amino Acid
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Son of Sevenless Proteins
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Spectrin / chemistry
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Type C Phospholipases / chemistry
Substances
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Blood Proteins
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Membrane Proteins
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Phosphoproteins
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Proteins
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Son of Sevenless Proteins
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platelet protein P47
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Spectrin
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Protein-Tyrosine Kinases
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Type C Phospholipases
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GTP Phosphohydrolases
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Dynamins