Cited by 602Protein Kinase Regulation and GTPase SignalingProtein Structure and DynamicsProtein Tyrosine Phosphatases

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

Zhang, Faming, Strand, Arne, Robbins, David, Cobb, Melanie H., Goldsmith, Elizabeth J.·1994·Nature

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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.

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Authors: Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J.
Affiliations: The University of Texas Southwestern Medical Center (US)
Howard Hughes Medical Institute (US)
ORCID: Robbins, David
Cobb, Melanie H.
Goldsmith, Elizabeth J.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1994-02
Volume: 367
Issue: 6465
Pages: 704-711
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/367704a0
OpenAlex: W1994954884
Cited by: 592
References: 52
Citations by year: 2026: 7 · 2025: 5 · 2024: 6 · 2023: 14 · 2022: 4 · 2021: 6 · 2020: 11 · 2019: 16 · 2018: 4 · 2017: 3 · 2016: 9 · 2015: 14 · 2014: 14 · 2013: 10 · 2012: 14
FWCI: 20.95
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: ERK2, mitogen-activated protein kinase, protein kinase structure, peptide binding site, conformational change, Ras/Raf signaling, kinase activation
MeSH terms: Adenosine Triphosphate, Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Phosphorylation, Protein Conformation, Substrate Specificity, Sequence Alignment, Calcium-Calmodulin-Dependent Protein Kinases, Crystallography, X-Ray, Mitogen-Activated Protein Kinase 1

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

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