5UOJ

THE STRUCTURE OF THE MAP KINASE P38 AT 2.1 ANGSTROMS RESOLUTION

Replaces:  1P38

Summary for 5UOJ

• Entry DOI: 10.2210/pdb5uoj/pdb
• Descriptor: Mitogen-activated protein kinase 14 (2 entities in total)
• Functional Keywords: transferase, map, kinase, p38
• Biological source: Mus musculus (Mouse)
• Cellular location: Cytoplasm : P47811
• Total number of polymer chains: 1
• Total formula weight: 43378.31

Authors

CHLEBOWICZ, J.,WANG, Z.,GOLDSMITH, E.J. (deposition date: 2017-01-31, release date: 2017-02-22, Last modification date: 2023-10-04)

Primary citation

Wang, Z.,Harkins, P.C.,Ulevitch, R.J.,Han, J.,Cobb, M.H.,Goldsmith, E.J.
The structure of mitogen-activated protein kinase p38 at 2.1-A resolution.
Proc. Natl. Acad. Sci. U.S.A., 94:2327-2332, 1997

PubMed Abstract: The structure of mitogen-activated protein (MAP) kinase p38 has been solved at 2.1-A 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.

PubMed: 9122194

Experimental method

X-RAY DIFFRACTION (2.1 Å)