ArticleStructure (London, England : 1993)2016
Dynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its Activity.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Host immune network-guided reverse vaccinology approach for prioritizing candidate antigens in Schistosoma japonicum-associated liver fibrosis.PLoS neglected tropical diseases · 2026Article
- An intramolecular energetic network regulates ligand recognition in a SH2 domain.Protein science : a publication of the Protein Society · 2023Article
- Fyn nanoclustering requires switching to an open conformation and is enhanced by FTLD-Tau biomolecular condensates.Molecular psychiatry · 2023Article
- The dynamics of free and phosphopeptide-bound Grb2-SH2 reveals two dynamically independent subdomains and an encounter complex with fuzzy interactions.Scientific reports · 2020Article
- Dynamic regulatory features of the protein tyrosine kinases.Biochemical Society transactions · 2019Review
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Authors and funding
8 authors.
Funding
Abstract
Src kinase activity is controlled by various mechanisms involving a coordinated movement of kinase and regulatory domains. Notwithstanding the extensive knowledge related to the backbone dynamics, little is known about the more subtle side-chain dynamics within the regulatory domains and their role in the activation process. Here, we show through experimental methyl dynamic results and predicted changes in side-chain conformational couplings that the SH2 structure of Fyn contains a dynamic network capable of propagating binding information. We reveal that binding the phosphorylated tail of Fyn perturbs a residue cluster near the linker connecting the SH2 and SH3 domains of Fyn, which is known to be relevant in the regulation of the activity of Fyn. Biochemical perturbation experiments validate that those residues are essential for inhibition of Fyn, leading to a gain of function upon mutation. These findings reveal how side-chain dynamics may facilitate the allosteric regulation of the different members of the Src kinase family.
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Registered trials
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