6APX

Crystal structure of human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the monobody YSX1

6APX の概要

• エントリーDOI: 10.2210/pdb6apx/pdb
• 分子名称: Maltose-binding periplasmic protein,Dual specificity protein phosphatase 1, Monobody YSX1, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: dual specificity phosphatase, dusp, c258s, hydrolase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Nucleus : P28562
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67899.48

構造登録者

Gumpena, R.,Lountos, G.T.,Sreejith, R.K.,Tropea, J.E.,Cherry, S.,Waugh, D.S. (登録日: 2017-08-18, 公開日: 2017-11-01, 最終更新日: 2023-10-04)

主引用文献

Gumpena, R.,Lountos, G.T.,Raran-Kurussi, S.,Tropea, J.E.,Cherry, S.,Waugh, D.S.
Crystal structure of the human dual specificity phosphatase 1 catalytic domain.
Protein Sci., 27:561-567, 2018

PubMed Abstract: The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2, JNK1 and p38-alpha. Here, we report the crystal structure of the human DUSP1 catalytic domain at 2.49 Å resolution. Uniquely, the protein was crystallized as an MBP fusion protein in complex with a monobody that binds to MBP. Sulfate ions occupy the phosphotyrosine and putative phosphothreonine binding sites in the DUSP1 catalytic domain.

PubMed: 29052270
DOI: 10.1002/pro.3328

実験手法

X-RAY DIFFRACTION (2.491 Å)