3P4K

The third conformation of p38a MAP kinase observed in phosphorylated p38a and in solution

Summary for 3P4K

• Entry DOI: 10.2210/pdb3p4k/pdb
• Descriptor: Mitogen-activated protein kinase 14, MAP kinase 14 (3 entities in total)
• Functional Keywords: kinase, phosphorylation, transferase
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm: P47811
• Total number of polymer chains: 2
• Total formula weight: 43734.93

Authors

Akella, R.,Min, X.,Wu, Q.,Gardner, K.H.,Goldsmith, E.J. (deposition date: 2010-10-06, release date: 2011-01-05, Last modification date: 2024-10-09)

Primary citation

Akella, R.,Min, X.,Wu, Q.,Gardner, K.H.,Goldsmith, E.J.
The third conformation of p38a MAP kinase observed in phosphorylated p38a and in solution
Structure, 18:1571-1578, 2010

PubMed 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/T∗GY∗/pepMEK3b) reveal a structure similar to unphosphorylated p38α/MEK3b, and distinct from phosphorylated p38γ (p38γ/T∗GY∗) and ERK2 (ERK2/T∗EY∗). The structure supports the idea that MAP kinases adopt three distinct conformations: unphosphorylated, phosphorylated, and a docking peptide-induced form.

PubMed: 21134636
DOI: 10.1016/j.str.2010.09.015

Experimental method

X-RAY DIFFRACTION (2.304 Å)