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- W2052021870 endingPage "710" @default.
- W2052021870 startingPage "698" @default.
- W2052021870 abstract "Phosphoinositides (PIs) are a group of key signaling and structural lipid molecules involved in a myriad of cellular processes. PI phosphatases, together with PI kinases, are responsible for the conversion of PIs between distinctive phosphorylation states. PI phosphatases are a large collection of enzymes that are evolved from at least two disparate ancestors. One group is distantly related to endonucleases, which apply divalent metal ions for phosphoryl transfer. The other group is related to protein tyrosine phosphatases, which contain a highly conserved active site motif Cys-X5-Arg (CX5R). In this review, we focus on structural insights to illustrate current understandings of the molecular mechanisms of each PI phosphatase family, with emphasis on their structural basis for substrate specificity determinants and catalytic mechanisms. This article is part of a Special Issue entitled Phosphoinositides." @default.
- W2052021870 created "2016-06-24" @default.
- W2052021870 creator A5039562453 @default.
- W2052021870 creator A5091440576 @default.
- W2052021870 date "2015-06-01" @default.
- W2052021870 modified "2023-10-13" @default.
- W2052021870 title "The structure of phosphoinositide phosphatases: Insights into substrate specificity and catalysis" @default.
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