Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 2001.06a
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- Pages.20-20
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- 2001
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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