Crystal Structure of the PTEN Tumor Suppressor: Implications for Its Phosphoinositide Phosphatase Activity and Membrane Association

  • Lee, Jie-Oh (Department of Chemistry, Korea Advanced Institute of Science and Technology) ;
  • Haijuan Yang (Memorial Sloan Kettering Cancer Center and Howard Hughes Medical Institut) ;
  • Nikola Pavletich (Memorial Sloan Kettering Cancer Center and Howard Hughes Medical Institute)
  • Published : 2001.06.01

Abstract

The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary cancer predisposition syndromes. PTEN is a phosphatase that can act on both polypeptide and phosphoinositide substrates in vitro. The PTEN structure reveals a phosphatase domain similar to protein phosphatases but having an enlarged active site important for the accommodation of the phosphoinositide substrate.(omitted)

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