1TZD

CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF INOSITOL 1,4,5-TRISPHOSPHATE 3-KINASE

1TZD の概要

• エントリーDOI: 10.2210/pdb1tzd/pdb
• 分子名称: Inositol-trisphosphate 3-kinase A, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: inositol kinase, transferase
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64460.90

構造登録者

Miller, G.J.,Hurley, J.H. (登録日: 2004-07-09, 公開日: 2004-09-21, 最終更新日: 2024-11-20)

主引用文献

Miller, G.J.,Hurley, J.H.
Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase
Mol.Cell, 15:703-711, 2004

PubMed Abstract: Soluble inositol polyphosphates are ubiquitous second messengers in eukaryotes, and their levels are regulated by an array of specialized kinases. The structure of an archetypal member of this class, inositol 1,4,5-trisphosphate 3-kinase (IP3K), has been determined at 2.2 angstroms resolution in complex with magnesium and adenosine diphosphate. IP3K contains a catalytic domain that is a variant of the protein kinase superfamily, and a novel four-helix substrate binding domain. The two domains are in an open conformation with respect to each other, suggesting that substrate recognition and catalysis by IP3K involves a dynamic conformational cycle. The unique helical domain of IP3K blocks access to the active site by membrane-bound phosphoinositides, explaining the structural basis for soluble inositol polyphosphate specificity.

PubMed: 15350215
DOI: 10.1016/j.molcel.2004.08.005

実験手法

X-RAY DIFFRACTION (2.2 Å)