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The Structure of Mitogen-Activated Protein Kinase p38 at 2.1- angstrom Resolution
Zhulun Wang, Paul C. Harkins, Richard J. Ulevitch, Jiahuai Han, Melanie H. Cobb and Elizabeth J. Goldsmith
Proceedings of the National Academy of Sciences of the United States of America
Vol. 94, No. 6 (Mar. 18, 1997), pp. 2327-2332
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/41637
Page Count: 6
You can always find the topics here!Topics: Phosphorylation, Binding sites, Proteins, Molecules, Active sites, Substrate specificity, Crystals, Biophysics, Atoms, Crossovers
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The structure of mitogen-activated protein (MAP) kinase p38 has been solved at 2.1- angstrom 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.
Proceedings of the National Academy of Sciences of the United States of America © 1997 National Academy of Sciences