The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
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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“MAPKs have a bi-lobed architecture, with a five-stranded b-sheet in the N-terminal lobe and six a-helices in the C-terminal lobe.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [18]
In the citing paper
“The MAPKs are activated via dual phosphorylation of a TPY motif found in the activation loop (A-loop), which connects the two lobes common to the kinase domain (Zhang et al., 1994) (Figure 1A).”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Zhang et al., 1994
Citations
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Sorted by citations
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
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A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells
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The Conformational Plasticity of Protein Kinases
Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,760
Metadata
- 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)
- Venue
- Nature
- Published
- 1994-02
- Volume
- 367
- Issue
- 6465
- Pages
- 704-711
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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