The structure of mitogen-activated protein kinase p38 at 2.1-A resolution.
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ABSTRACT:
SUBMITTER: Wang Z
PROVIDER: S-EPMC20087 | biostudies-other | 1997 Mar
REPOSITORIES: biostudies-other
Publications
The structure of mitogen-activated protein kinase p38 at 2.1-A resolution.
Wang Z Z Harkins P C PC Ulevitch R J RJ Han J J Cobb M H MH Goldsmith E J EJ
Proceedings of the National Academy of Sciences of the United States of America 19970301 6
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 activat ...[more]
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2022-05-06 | GSE184361 | GEO