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4CML

Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate

4CML の概要
エントリーDOI10.2210/pdb4cml/pdb
関連するPDBエントリー4CMN
分子名称TYPE II INOSITOL 1,4,5-TRISPHOSPHATE 5- PHOSPHATASE, ISOFORM 2, 1,2-dioctanoyl phosphatidyl epi-inositol (3,4)-bisphosphate, MAGNESIUM ION, ... (7 entities in total)
機能のキーワードhydrolase, sgc, signalling, structural genomics consortium stockholm, magnesium binding
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Cytoplasm, cytosol : P32019
タンパク質・核酸の鎖数1
化学式量合計37195.57
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-, 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 (2.3 Å)
構造検証レポート
Validation report summary of 4cml
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2026-01-28に公開中

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