title: Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases.
abstract: In this issue of Structure, Trésaugues and colleagues determined the interaction of membrane-bound phosphoinositides with three clinically significant human inositol polyphosphate 5-phosphatases (I5Ps). A comparison to the structures determined with soluble substrates revealed differences in the binding mode and suggested how the I5Ps and apurinic endonuclease (APE1) activities evolved from the same metal-binding active center.
authors.affiliation: Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, USA; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA. Electronic address: webraun@utmb.edu.
authors.forename: Werner
authors.initials: W
authors.lastname: Braun
authors.affiliation: Foundation for Applied Molecular Evolution, 720 SW 2nd Avenue Suite 201, Gainesville, FL 32601, USA.
authors.forename: Catherine H
authors.initials: CH
authors.lastname: Schein
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D000072183:Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D000099182:Phosphoinositide 5-Phosphatases
chemical_list: D000072183:Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases; D010744:Phosphoric Monoester Hydrolases; D000099182:Phosphoinositide 5-Phosphatases; C075695:OCRL protein, human; C098706:INPPL1 protein, human