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Crystal Structures of MAP Kinase p38 Complexed to the Docking Sites on Its Nuclear Substrate MEF2A and Activator MKK3b
Open accessAbstract
The structures of the MAP kinase p38 in complex with docking site peptides containing a phi(A)-X-phi(B) motif, derived from substrate MEF2A and activating enzyme MKK3b, have been solved. The peptides bind to the same site in the C-terminal domain of the kinase, which is both outside the active site and distinct from the "CD" domain previously implicated in docking site interactions. Mutational analysis on the interaction of p38 with the docking sites supports the crystallographic models and has uncovered two novel residues on the docking groove that are critical for binding. The two peptides induce similar large conformational changes local to the peptide binding groove. The peptides also induce unexpected and different conformational changes in the active site, as well as structural disorder in the phosphorylation lip.
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In the citing paper
“The first crystal structures of a MAPK, p38, bound to a KIM peptide (MEF2A, a substrate, and MKK3b, an activating kinase) were described in 2002 by the Goldsmith laboratory.42”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [42]
In the citing paper
“Allostery among the catalytic site, A-loop, and peptide-docking site of ERK and p38 MAPKs has been well documented (Chang et al., 2002; Goldsmith, 2011; Lee et al., 2004; Wang et al., 1997; Zhang et al., 1994; Zhou et al., 2006a, 2006b), but much less is known about these processes for JNK.”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Chang et al., 2002
In the citing paper
“At the structural level, MAPK docking is a well characterized protein-peptide interaction system (9, 12-16).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [9]
In the citing paper
“For example, MAPKs phosphorylate serine and threonine residues that are followed by proline (called a S/TP target site or motif) and they also bind to docking (D)-motifs, which are ~8-12 amino acid long fragments satisfying a loose consensus sequence (9)”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [9]
In the citing paper
“Similarly to the previously determined structures of the p38α-pepMEF2A and p38α-pepMKK3 complexes, the N-terminal region of the MKK6 D-motif cannot be seen on the electron density map of the pepMKK6-p38α complex (9).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [9]
In the citing paper
“Docking motifs from these three proteins bind the MAPK docking groove (9,12,22).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [9]
In the citing paper
“In this structure, it is found that the docking site of the scaffolding protein also binds at the same docking grooves of JNK1 as the upstream kinase and the substrate transcription factor do in p38 MAPK (Chang et al , 2002), but with quite different interaction modes.”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Chang et al , 2002
In the citing paper
“the overall conformations and binding positions of the bound peptides are quite different from each other when the structures of JNK1 and p38 are superimposed”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Chang et al , 2002
In the citing paper
“the similar increased disorder of the phosphorylation loop of p38 MAPK was also found when MEF2A or MKK3b peptide binds (Chang et al , 2002).”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Chang et al , 2002
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Metadata
- Authors
- Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Goldsmith, Elizabeth J
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2002-06
- Volume
- 9
- Issue
- 6
- Pages
- 1241-1249
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2017012572
- Cited by
- 302
- References
- 42
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2 · 2023: 7 · 2022: 2 · 2021: 8 · 2020: 12 · 2019: 9 · 2018: 6 · 2017: 10 · 2016: 13 · 2015: 7 · 2014: 7 · 2013: 15 · 2012: 11
- FWCI
- 8.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 46993, R01DK046993)
- 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 Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- MEF2A, docking site, kinase-substrate interactions, C-terminal domain, peptide binding groove, conformational change, MAPK activation
- MeSH terms
- Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Cell Line, DNA-Binding Proteins, Humans, Models, Molecular, Molecular Sequence Data, Peptides, Protein-Tyrosine Kinases, Transcription Factors, Molecular Structure, Mutagenesis, Site-Directed, Myogenic Regulatory Factors, Crystallography, X-Ray, Protein Structure, Quaternary, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, MADS Domain Proteins, p38 Mitogen-Activated Protein Kinases, MAP Kinase Kinase 3, MEF2 Transcription Factors
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