Journal
CELL
Volume 105, Issue 3, Pages 379-389Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(01)00326-9
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Inositol polyphosphate 5-phosphatases are central to intracellular processes ranging from membrane trafficking to Ca2+ signaling, and defects in this activity result in the human disease Lowe syndrome. The 1.8 Angstrom resolution structure of the inositol polyphosphate 5-phosphatase domain of SPsynaptojanin bound to Ca2+ and inositol (1,4)-bisphosphate reveals a fold and an active site His and Asp pair resembling those of several Mg2+-dependent nucleases. Additional loops mediate specific inositol polyphosphate contacts. The 4-phosphate of inositol (1,4)-bisphosphate is misoriented by 4.6 Angstrom compared to the reactive geometry observed in the apurinic/apyrimidinic endonuclease 1, explaining the dephosphorylation site selectivity of the 5-phosphatases. Based on the structure, a series of mutants are described that exhibit altered substrate specificity providing general determinants for substrate recognition.
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