3NR8
Crystal structure of human SHIP2
3NR8 の概要
エントリーDOI | 10.2210/pdb3nr8/pdb |
関連するPDBエントリー | 3MTC 3N9V |
分子名称 | Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2, CHLORIDE ION (3 entities in total) |
機能のキーワード | structural genomics consortium, sgc, phosphatidylinositol-3, 4, 5-trisphosphate 5-phosphatase 2, ship2, inppl1, ship-2, phosphatidylinositol, phosphatase, signalling, magnesium, structural genomics consortium stockholm, magnesium binding, hydrolase |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Cytoplasm, cytosol: O15357 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 72523.16 |
構造登録者 | Tresaugues, L.,Welin, M.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, I.,Karlberg, T.,Kol, S.,Kotenyova, T.,Kouznetsova, E.,Moche, M.,Nyman, T.,Persson, C.,Schuler, H.,Schutz, P.,Siponen, M.I.,Thorsell, A.G.,van der Berg, S.,Wahlberg, E.,Weigelt, J.,Nordlund, P.,Structural Genomics Consortium (SGC) (登録日: 2010-06-30, 公開日: 2010-08-25, 最終更新日: 2023-09-06) |
主引用文献 | Tresaugues, L.,Silvander, C.,Flodin, S.,Welin, M.,Nyman, T.,Graslund, S.,Hammarstrom, M.,Berglund, H.,Nordlund, P. Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases Structure, 22:744-755, 2014 Cited by PubMed Abstract: SHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase subfamilies involved in insulin regulation and Lowes syndrome. The structural basis for membrane recognition, substrate specificity, and regulation of inositol polyphosphate 5-phophatases is still poorly understood. We determined the crystal structures of human SHIP2, OCRL, and INPP5B, the latter in complex with phosphoinositide substrate analogs, which revealed a membrane interaction patch likely to assist in sequestering substrates from the lipid bilayer. Residues recognizing the 1-phosphate of the substrates are highly conserved among human family members, suggesting similar substrate binding modes. However, 3- and 4-phosphate recognition varies and determines individual substrate specificity profiles. The high conservation of the environment of the scissile 5-phosphate suggests a common reaction geometry for all members of the human 5-phosphatase family. PubMed: 24704254DOI: 10.1016/j.str.2014.01.013 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
構造検証レポート
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