Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

Faming Zhang, Arne Strand, David Robbins, Melanie H. Cobb, Elizabeth J. Goldsmith

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Abstract

The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.

Original languageEnglish (US)
Pages (from-to)704-711
Number of pages8
JournalNature
Volume367
Issue number6465
DOIs
StatePublished - Jan 1 1994

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Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994). Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature, 367(6465), 704-711. https://doi.org/10.1038/367704a0