1D5R

Crystal Structure of the PTEN Tumor Suppressor

1D5R の概要

• エントリーDOI: 10.2210/pdb1d5r/pdb
• 分子名称: PHOSPHOINOSITIDE PHOSPHATASE PTEN, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: c2 domain, phosphotidylinositol, phosphatase, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm . Isoform alpha: Secreted : P60484
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38646.27

構造登録者

Lee, J.O.,Yang, H.,Georgescu, M.-M.,Di Cristofano, A.,Pavletich, N.P. (登録日: 1999-10-11, 公開日: 1999-11-04, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)