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lüll The PX domain: a new phosphoinositide-binding module Ellson CD; Andrews S; Stephens LR; Hawkins PTJ Cell Sci 2002[Mar]; 115 (Pt 6): 1099-105The PX domain, which until recently was an orphan domain, has emerged as the latest member of the phosphoinositide-binding module superfamily. Structural studies have revealed that it has a novel fold and identified key residues that interact with the bound phosphoinositide, enabling some prediction of phosphoinositide-binding specificity. Specificity for PtdIns(3)P appears to be the most common, and several proteins containing PX domains localise to PtdIns(3)P-rich endosomal and vacuolar structures through their PX domains: these include the yeast t-SNARE Vam7p, mammalian sorting nexins (involved in membrane trafficking events) and the Ser/Thr kinase CISK, which is implicated in cell survival. Additionally, phosphoinositide binding to the PX domains of p40(phox) and p47(phox) appears to play a critical role in the active assembly of the neutrophil oxidase complex.|Binding Sites[MESH]|Carrier Proteins/metabolism[MESH]|Endosomes/metabolism[MESH]|Eye Proteins/metabolism[MESH]|Fatty Acid-Binding Proteins[MESH]|Models, Molecular[MESH]|Phagosomes/metabolism[MESH]|Phosphatidylinositol Phosphates/metabolism[MESH]|Phosphatidylinositols/*metabolism[MESH]|Protein Structure, Tertiary[MESH]|Vacuoles/metabolism[MESH]|src Homology Domains[MESH] |