6C01
Human ectonucleotide pyrophosphatase / phosphodiesterase 3 (ENPP3, NPP3, CD203c)
6C01 の概要
エントリーDOI | 10.2210/pdb6c01/pdb |
分子名称 | Ectonucleotide pyrophosphatase/phosphodiesterase family member 3, CALCIUM ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total) |
機能のキーワード | phosphodiesterase, nucleotide, zinc, hydrolase |
由来する生物種 | Homo sapiens (Human) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 203612.14 |
構造登録者 | Gorelik, A.,Randriamihaja, A.,Illes, K.,Nagar, B. (登録日: 2017-12-27, 公開日: 2018-05-02, 最終更新日: 2024-10-23) |
主引用文献 | Gorelik, A.,Randriamihaja, A.,Illes, K.,Nagar, B. Structural basis for nucleotide recognition by the ectoenzyme CD203c. FEBS J., 285:2481-2494, 2018 Cited by PubMed Abstract: The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides. CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells. Multiple other roles and substrates have also been proposed for this protein. In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog. The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands. Dimerization of the protein does not affect its catalytic activity. These findings expand our understanding of substrate recognition within the NPP family. PubMed: 29717535DOI: 10.1111/febs.14489 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
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