2GPH

Docking motif interactions in the MAP kinase ERK2

2GPH の概要

• エントリーDOI: 10.2210/pdb2gph/pdb
• 分子名称: Mitogen-activated protein kinase 1, Tyrosine-protein phosphatase non-receptor type 7 (3 entities in total)
• 機能のキーワード: erk2, docking interaction, d-motif, allostery, cd-site, phosphatase-derived peptide, processing conformation, transferase
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle : P63086; Cytoplasm : P35236
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44025.65

構造登録者

Zhou, T.,Sun, L.,Humphreys, J.,Goldsmith, E.J. (登録日: 2006-04-17, 公開日: 2006-07-04, 最終更新日: 2024-11-06)

主引用文献

Zhou, T.,Sun, L.,Humphreys, J.,Goldsmith, E.J.
Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2.
Structure, 14:1011-1019, 2006

PubMed Abstract: MAP kinases bind activating kinases, phosphatases, and substrates through docking interactions. Here, we report a 1.9 A crystallographic analysis of inactive ERK2 bound to a "D motif" docking peptide (pepHePTP) derived from hematopoietic tyrosine phosphatase, a negative regulator of ERK2. In this complex, the complete D motif interaction defined by mutagenic analysis is observed, including extensive electrostatic interactions with the "CD" site of the kinase. Large conformational changes occur in the activation loop where the dual phosphorylation sites, which are buried in the inactive form of ERK2, become exposed to solvent in the complex. Similar conformational changes occur in a complex between ERK2 and a MEK2 (MAP/ERK kinase-2)-derived D motif peptide (pepMEK2). D motif peptides are known to bind homologous loci in the MAP kinases p38alpha and JNK1, also inducing conformational changes in these enzymes. However, the binding interactions and conformational changes are unique to each, thus contributing to specificity among MAP kinases.

PubMed: 16765894
DOI: 10.1016/j.str.2006.04.006

実験手法

X-RAY DIFFRACTION (1.9 Å)