The third conformation of p38α MAP kinase observed in phosphorylated p38α and in solution

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Abstract

MAPKs engage substrates, MAP2Ks, and phosphatases via a docking groove in the C-terminal domain of the kinase. Prior crystallographic studies on the unphosphorylated MAPKs p38α and ERK2 defined the docking groove and revealed long-range conformational changes affecting the activation loop and active site of the kinase induced by peptide. Solution NMR data presented here for unphosphorylated p38α with a MEK3b-derived peptide (p38α/pepMEK3b) validate these findings. Crystallograhic data from doubly phosphorylated active p38α (p38α/TGY/pepMEK3b) reveal a structure similar to unphosphorylated p38α/MEK3b, and distinct from phosphorylated p38γ (p38γ/TGY) and ERK2 (ERK2/TEY). The structure supports the idea that MAP kinases adopt three distinct conformations: unphosphorylated, phosphorylated, and a docking peptide-induced form.

Original languageEnglish (US)
Pages (from-to)1571-1578
Number of pages8
JournalStructure
Volume18
Issue number12
DOIs
StatePublished - Dec 8 2010

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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