The PH superfold: a structural scaffold for multiple functions.
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.
Blomberg
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European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 10.2209, D-690 12 Heidelberg, Germany.
Baraldi
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Nilges
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Saraste
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D020816:Amino Acid Motifs; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D008024:Ligands; D010716:Phosphatidylinositols / Q000378:metabolism; D010750:Phosphoproteins; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D013329:Structure-Activity Relationship
D001798:Blood Proteins; D008024:Ligands; D010716:Phosphatidylinositols; D010750:Phosphoproteins; C039077:platelet protein P47