1LW3

Crystal Structure of Myotubularin-related protein 2 complexed with phosphate

1LW3 の概要

• エントリーDOI: 10.2210/pdb1lw3/pdb
• 分子名称: Myotubularin-related protein 2, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: protein-phosphate complex, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q13614
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 75291.65

構造登録者

Begley, M.J.,Taylor, G.S.,Kim, S.-A.,Veine, D.M.,Dixon, J.E.,Stuckey, J.A. (登録日: 2002-05-30, 公開日: 2003-10-07, 最終更新日: 2024-02-14)

主引用文献

Begley, M.J.,Taylor, G.S.,Kim, S.-A.,Veine, D.M.,Dixon, J.E.,Stuckey, J.A.
Crystal Structure of a Phosphoinositide Phosphatase, MTMR2: Insights into Myotubular Myopathy and Charcot-Marie-Tooth Syndrome
Mol.Cell, 12:1391-1402, 2003

PubMed Abstract: Myotubularin-related proteins are a large subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in members of the myotubularin family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. The crystal structure of a representative member of this family, MTMR2, reveals a phosphatase domain that is structurally unique among PTPs. A series of mutants are described that exhibit altered enzymatic activity and provide insight into the specificity of myotubularin phosphatases toward phosphoinositide substrates. The structure also reveals that the GRAM domain, found in myotubularin family phosphatases and predicted to occur in approximately 180 proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. Finally, the MTMR2 structure will serve as a model for other members of the myotubularin family and provide a framework for understanding the mechanism whereby mutations in these proteins lead to disease.

PubMed: 14690594
DOI: 10.1016/S1097-2765(03)00486-6

実験手法

X-RAY DIFFRACTION (2.3 Å)