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Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

Nature volume 367, pages 704–711 (1994)Cite this article

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.

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Authors and Affiliations

  1. Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, USA

    Faming Zhang & Elizabeth J. Goldsmith

  2. Department of Pharmacology, The University of Texas Southwestern Medical Center at Dallas, USA

    David Robbins & Melanie H. Cobb

  3. Howard Hughes Medical Institute, 5323 Harry Hines Boulevard, Dallas, Texas, 75235, USA

    Arne Strand

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  1. Faming Zhang
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  2. Arne Strand
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  3. David Robbins
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  4. Melanie H. Cobb
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  5. Elizabeth J. Goldsmith
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Zhang, F., Strand, A., Robbins, D. et al. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704–711 (1994). https://doi.org/10.1038/367704a0

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