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Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases.
SHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase subfamilies involved in insulin regulation and Lowes syndrome. The structural basis for membrane recognition, substrate… Expand
Crystal Structures of Type-II Inositol Polyphosphate 5-Phosphatase INPP5B with Synthetic Inositol Polyphosphate Surrogates Reveal New Mechanistic Insights for the Inositol 5-Phosphatase Family
- S. Mills, C. Silvander, G. Cozier, L. Trésaugues, P. Nordlund, B. Potter
- Chemistry, Medicine
- 8 February 2016
The inositol polyphosphate 5-phosphatase INPP5B hydrolyzes the 5-phosphate group from water- and lipid-soluble signaling messengers. Two synthetic benzene and biphenyl polyphosphates (BzP/BiPhPs),… Expand
Structural Basis for the Specificity of Human NUDT16 and Its Regulation by Inosine Monophosphate
Human NUDT16 is a member of the NUDIX hydrolase superfamily. After having been initially described as an mRNA decapping enzyme, recent studies conferred it a role as an “housecleaning” enzyme… Expand
Crystal structure of INPP5B in complex with benzene 1,2,4,5- tetrakisphosphate
Complex between MTH1 and compound 29 (a 4-amino-2,7-diazaindole derivative)
Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate
Crystal structure of OCRL in complex with a phosphate ion
Complex between MTH1 and compound 7 (a 7-azaindole-2-amide derivative)
Complex between MTH1 and compound 1 (a 7-azaindole-4-ester derivative)