Phosphoinositide phosphatase
From Proteopedia
FunctionPhosphoinositide phosphatase degrades phosphoinositide signals[1]. PTEN is phosphatidylinositol 3,4,5-triphosphate 3-phosphatase and dual-specificity protein phosphatase. For details of PTEN phosphatase see DiseaseMutations in the Sac phosphatase lead to degenerative neuropathy[2]. Structural highlightsThe substrate binds to one terminus of the β sandwich. Alpha Helices, Beta Strands , Loops , Turns. Substrate phosphoinositol 4-phospate binding site. Water molecules are shown as red spheres. Cl- coordination site (PDB code 3mtc).[3]
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3D Structures of phosphoinositide phosphatase
Updated on 04-August-2019
References
- ↑ Dyson JM, Fedele CG, Davies EM, Becanovic J, Mitchell CA. Phosphoinositide phosphatases: just as important as the kinases. Subcell Biochem. 2012;58:215-79. doi: 10.1007/978-94-007-3012-0_7. PMID:22403078 doi:http://dx.doi.org/10.1007/978-94-007-3012-0_7
- ↑ Liu Y, Bankaitis VA. Phosphoinositide phosphatases in cell biology and disease. Prog Lipid Res. 2010 Jul;49(3):201-17. doi: 10.1016/j.plipres.2009.12.001. Epub, 2010 Jan 5. PMID:20043944 doi:http://dx.doi.org/10.1016/j.plipres.2009.12.001
- ↑ Tresaugues L, Silvander C, Flodin S, Welin M, Nyman T, Graslund S, Hammarstrom M, Berglund H, Nordlund P. Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases. Structure. 2014 Apr 2. pii: S0969-2126(14)00073-2. doi:, 10.1016/j.str.2014.01.013. PMID:24704254 doi:http://dx.doi.org/10.1016/j.str.2014.01.013