Structural highlights
Publication Abstract from PubMed
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 p38alpha 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 p38alpha with a MEK3b-derived peptide (p38alpha/pepMEK3b) validate these findings. Crystallograhic data from doubly phosphorylated active p38alpha (p38alpha/T *GY */pepMEK3b) reveal a structure similar to unphosphorylated p38alpha/MEK3b, and distinct from phosphorylated p38gamma (p38gamma/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.
The third conformation of p38alpha MAP kinase observed in phosphorylated p38alpha and in solution.,Akella R, Min X, Wu Q, Gardner KH, Goldsmith EJ Structure. 2010 Dec 8;18(12):1571-8. PMID:21134636[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Akella R, Min X, Wu Q, Gardner KH, Goldsmith EJ. The third conformation of p38alpha MAP kinase observed in phosphorylated p38alpha and in solution. Structure. 2010 Dec 8;18(12):1571-8. PMID:21134636 doi:10.1016/j.str.2010.09.015
