title: The PH superfold: a structural scaffold for multiple functions.
abstract: 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.
authors.affiliation: European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 10.2209, D-690 12 Heidelberg, Germany.
authors.forename: N
authors.initials: N
authors.lastname: Blomberg
authors.forename: E
authors.initials: E
authors.lastname: Baraldi
authors.forename: M
authors.initials: M
authors.lastname: Nilges
authors.forename: M
authors.initials: M
authors.lastname: Saraste
mesh_terms: 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
chemical_list: D001798:Blood Proteins; D008024:Ligands; D010716:Phosphatidylinositols; D010750:Phosphoproteins; C039077:platelet protein P47