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3NR8

Crystal structure of human SHIP2

3NR8 の概要
エントリーDOI10.2210/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
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: 24704254
DOI: 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
Validation report summary of 3nr8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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