MAP kinase p38

The structure of the MAP kinase p38 has been solved, the second MAP kinase structure determined in the low activity conformation. While p38 is topologically similar to the MAP kinase ERK2, key regions of the structure, the phosphorylation Lip, the peptide substrate binding site, and the ATP binding site are different, explaining 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.

The structure of the MAP kinase p38 at 2.1Å resolution.

Zhulun Wang, Paul C Harkins, Richard J Ulevitch, Jiahuai Han, Melanie H Cobb and Elizabeth J Goldsmith.
PNAS, 94:2337-2332(1997)