3p4k | pdb_00003p4k
From Proteopedia
The third conformation of p38a MAP kinase observed in phosphorylated p38a and in solution
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Structural highlights
Publication Abstract from PubMedMAPKs 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 AlsoReferences
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This page was last modified 13:43, 9 December 2014.