Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

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

Research output: Contribution to journalArticle

496 Citations (Scopus)

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
Pages (from-to)704-711
Number of pages8
JournalNature
Volume367
Issue number6465
StatePublished - Feb 24 1994
Externally publishedYes

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Cyclic AMP-Dependent Protein Kinases
Protein Kinases
Tyrosine
Phosphotransferases
Binding Sites
Peptides
Enzymes

ASJC Scopus subject areas

  • General

Cite this

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

Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. / Zhang, Faming; Strand, Arne; Robbins, David J; Cobb, Melanie H.; Goldsmith, Elizabeth J.

In: Nature, Vol. 367, No. 6465, 24.02.1994, p. 704-711.

Research output: Contribution to journalArticle

Zhang, F, Strand, A, Robbins, DJ, Cobb, MH & Goldsmith, EJ 1994, 'Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution', Nature, vol. 367, no. 6465, pp. 704-711.
Zhang F, Strand A, Robbins DJ, Cobb MH, Goldsmith EJ. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature. 1994 Feb 24;367(6465):704-711.
Zhang, Faming ; Strand, Arne ; Robbins, David J ; Cobb, Melanie H. ; Goldsmith, Elizabeth J. / Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. In: Nature. 1994 ; Vol. 367, No. 6465. pp. 704-711.
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