ArticleThe Journal of biological chemistry2019
Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- The partner gene modulates response to asciminib in ABL1-rearranged Acute Lymphoblastic Leukemia.Neoplasia (New York, N.Y.) · 2026Article
- Definition and Discovery of Tandem SH3-Binding Motifs Interacting with Members of the p47Biomolecules · 2025Article
- Activity of STAMP inhibitors inBlood neoplasia · 2025Article
- Synthetic Phosphorylation Networks with Fluorescence and Luminescence Expansion.ACS synthetic biology · 2025Article
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- Characterization of the Intramolecular Interactions and Regulatory Mechanisms of the Scaffold Protein Tks4.International journal of molecular sciences · 2021Article
- Itk Promotes the Integration of TCR and CD28 Costimulation through Its Direct Substrates SLP-76 and Gads.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Review
- Article
- TMEA, a Polyphenol inFrontiers in cell and developmental biology · 2021Article
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Src homology 3 (SH3) domains bind proline-rich linear motifs in eukaryotes. By mediating inter- and intramolecular interactions, they regulate the functions of many proteins involved in a wide variety of signal transduction pathways. Phosphorylation at different tyrosine residues in SH3 domains has been reported previously. In several cases, the functional consequences have also been investigated. However, a full understanding of the effects of tyrosine phosphorylation on the ligand interactions and cellular functions of SH3 domains requires detailed structural, atomic-resolution studies along with biochemical and biophysical analyses. Here, we present the first crystal structures of tyrosine-phosphorylated human SH3 domains derived from the Abelson-family kinases ABL1 and ABL2 at 1.6 and 1.4 Å resolutions, respectively. The structures revealed that simultaneous phosphorylation of Tyr
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