1D5R

Crystal Structure of the PTEN Tumor Suppressor

Summary for 1D5R

• Entry DOI: 10.2210/pdb1d5r/pdb
• Descriptor: PHOSPHOINOSITIDE PHOSPHATASE PTEN, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: c2 domain, phosphotidylinositol, phosphatase, hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm . Isoform alpha: Secreted : P60484
• Total number of polymer chains: 1
• Total formula weight: 38646.27

Authors

Lee, J.O.,Yang, H.,Georgescu, M.-M.,Di Cristofano, A.,Pavletich, N.P. (deposition date: 1999-10-11, release date: 1999-11-04, Last modification date: 2024-02-07)

Primary citation

Lee, J.O.,Yang, H.,Georgescu, M.M.,Di Cristofano, A.,Maehama, T.,Shi, Y.,Dixon, J.E.,Pandolfi, P.,Pavletich, N.P.
Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association.
Cell(Cambridge,Mass.), 99:323-334, 1999

PubMed 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 that is similar to protein phosphatases but has an enlarged active site important for the accommodation of the phosphoinositide substrate. The structure also reveals that PTEN has a C2 domain. The PTEN C2 domain binds phospholipid membranes in vitro, and mutation of basic residues that could mediate this reduces PTEN's membrane affinity and its ability to suppress the growth of glioblastoma tumor cells. The phosphatase and C2 domains associate across an extensive interface, suggesting that the C2 domain may serve to productively position the catalytic domain on the membrane.

PubMed: 10555148
DOI: 10.1016/S0092-8674(00)81663-3

Experimental method

X-RAY DIFFRACTION (2.1 Å)