Abstract
Background: MAPK cascade proteins bind to each other selectively via docking interactions. Results: The high selectivity of JNK family MAPKs for cognate binding partners is controlled by two key hydrophobic residues in the docking site. Conclusion: This contrasts with other proposed models of docking specificity. Significance: This has implications for drug design and for the evolution of signaling specificity.
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CITATION STYLE
Jane Bardwell, A., & Bardwell, L. (2015). Two hydrophobic residues can determine the specificity of Mitogen-activated protein Kinase docking interactions. Journal of Biological Chemistry, 290(44), 26661–26674. https://doi.org/10.1074/jbc.M115.691436
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