1M3G

SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION

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1M3G の概要

• エントリーDOI: 10.2210/pdb1m3g/pdb
• NMR情報: BMRB: 5552
• 分子名称: DUAL SPECIFICITY PROTEIN PHOSPHATASE 2 (1 entity in total)
• 機能のキーワード: catalytic domain, mapk phosphatase, pac-1, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q05923
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16129.42

構造登録者

Farooq, A.,Zhou, M.-M. (登録日: 2002-06-27, 公開日: 2003-06-27, 最終更新日: 2024-05-22)

主引用文献

Farooq, A.,Plotnikova, O.,Chaturvedi, G.,Yan, S.,Zeng, L.,Zhang, Q.,Zhou, M.-M.
Solution Structure of the MAPK Phosphatase PAC-1 Catalytic Domain Insights into Substrate-Induced Enzymatic Activation of MKP
Structure, 11:155-164, 2003

PubMed Abstract: Inactivation of mitogen-activated protein kinases (MAPKs) by MAPK phosphatases (MKPs) is accomplished via substrate-induced activation of the latter enzymes; however, the structural basis for the underlying mechanism remains elusive. Here, we report the three-dimensional solution structure of the C-terminal phosphatase domain of the prototypical MKP PAC-1, determined when bound to phosphate. Structural and biochemical analyses reveal unique active site geometry of the enzyme important for binding to phosphorylated threonine and tyrosine of MAPK ERK2. Our study further demonstrates that the dynamic interaction between the N-terminal kinase binding domain and the C-terminal phosphatase domain of an MKP is directly coupled to MAPK-induced conformational change of the phosphatase active site, which is essential for eliciting its full enzymatic activity.

PubMed: 12575935
DOI: 10.1016/S0969-2126(02)00943-7

実験手法

SOLUTION NMR