ArticleActa crystallographica. Section D, Biological crystallography2013
Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Molecular basis of mitogen-activated protein kinase ERK2 activation by its upstream kinase MEK1.bioRxiv : the preprint server for biology · 2026Article
- Targeting ERK-MYD88 interaction leads to ERK dysregulation and immunogenic cancer cell death.Nature communications · 2024Article
- Linear motif specificity in signaling through p38α and ERK2 mitogen-activated protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Integrated Covalent Drug Design Workflow Using Site Identification by Ligand Competitive Saturation.Journal of chemical theory and computation · 2023Article
- Ancient MAPK ERK7 is regulated by an unusual inhibitory scaffold required forProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Targeting ERK beyond the boundaries of the kinase active site in melanoma.Molecular carcinogenesis · 2019Review
- The human Na(+)/H(+) exchanger 1 is a membrane scaffold protein for extracellular signal-regulated kinase 2.BMC biology · 2016Article
- Two hydrophobic residues can determine the specificity of mitogen-activated protein kinase docking interactions.The Journal of biological chemistry · 2015Article
- Mapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Co-conserved MAPK features couple D-domain docking groove to distal allosteric sites via the C-terminal flanking tail.PloS one · 2015Article
- Molecular basis of MAP kinase regulation.Protein science : a publication of the Protein Society · 2013Review
- Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module.The Journal of biological chemistry · 2013Article
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3 authors.
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Abstract
Linear motifs normally bind with only medium binding affinity (Kd of ∼0.1-10 µM) to shallow protein-interaction surfaces on their binding partners. The crystallization of proteins in complex with linear motif-containing peptides is often challenging because the energy gained upon crystal packing between symmetry mates in the crystal may be on a par with the binding energy of the protein-peptide complex. Furthermore, for extracellular signal-regulated kinase 2 (ERK2) the protein-peptide docking surface is comprised of a small hydrophobic surface patch that is often engaged in the crystal packing of apo ERK2 crystals. Here, a rational surface-engineering approach is presented that involves mutating protein surface residues that are distant from the peptide-binding ERK2 docking groove to alanines. These ERK2 surface mutations decrease the chance of `unwanted' crystal packing of ERK2 and the approach led to the structure determination of ERK2 in complex with new docking peptides. These findings highlight the importance of negative selection in crystal engineering for weakly binding protein-peptide complexes.
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