The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution
Z Wang, PC Harkins, RJ Ulevitch… - Proceedings of the …, 1997 - National Acad Sciences
Z Wang, PC Harkins, RJ Ulevitch, J Han, MH Cobb, EJ Goldsmith
Proceedings of the National Academy of Sciences, 1997•National Acad SciencesThe structure of mitogen-activated protein (MAP) kinase p38 has been solved at 2.1-Å to an
R factor of 21.0%, making p38 the second low activity MAP kinase solved to date. Although
p38 is topologically similar to the MAP kinase ERK2, the phosphorylation Lip (a regulatory
loop near the active site) adopts a different fold in p38. The peptide substrate binding site
and the ATP binding site are also different from those of ERK2. The results explain why MAP
kinases are specific for different activating enzymes, substrates, and inhibitors. A model …
R factor of 21.0%, making p38 the second low activity MAP kinase solved to date. Although
p38 is topologically similar to the MAP kinase ERK2, the phosphorylation Lip (a regulatory
loop near the active site) adopts a different fold in p38. The peptide substrate binding site
and the ATP binding site are also different from those of ERK2. The results explain why MAP
kinases are specific for different activating enzymes, substrates, and inhibitors. A model …
The structure of mitogen-activated protein (MAP) kinase p38 has been solved at 2.1-Å to an R factor of 21.0%, making p38 the second low activity MAP kinase solved to date. Although p38 is topologically similar to the MAP kinase ERK2, the phosphorylation Lip (a regulatory loop near the active site) adopts a different fold in p38. The peptide substrate binding site and the ATP binding site are also different from those of ERK2. The results explain why MAP kinases are specific for different activating enzymes, substrates, and inhibitors. A model presented for substrate and activator interactions has implications for the evolution of protein kinase cascades.
National Acad Sciences
