ArticleCell2008
Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.
Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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Who cites it
110 citing papers in PubMed.
- Lipid Pocket Binders Impose Allosteric Changes of Protein Dynamics Around the Active Site of the Protein Kinase p38α.Angewandte Chemie (International ed. in English) · 2026Article
- The Inositol-5-Phosphatase SHIP1: Expression, Regulation and Role in Acute Lymphoblastic Leukemia.International journal of molecular sciences · 2025Review
- Non-Receptor Tyrosine Kinases: Their Structure and Mechanistic Role in Tumor Progression and Resistance.Cancers · 2024Review
- Exploration of the carcinogenetic and immune role of CHK1 in human cancer.Journal of Cancer · 2024Article
- Computational analysis of regulatory regions in human protein kinases.Protein science : a publication of the Protein Society · 2023Article
- Article
- Allosteric regulation and inhibition of protein kinases.Biochemical Society transactions · 2023Review
- SRRM2 organizes splicing condensates to regulate alternative splicing.Nucleic acids research · 2022Article
- Engineered SH2 Domains for Targeted Phosphoproteomics.ACS chemical biology · 2022Article
- Characterization and clustering of kinase isoform expression in metastatic melanoma.PLoS computational biology · 2022Article
- Allosteric regulation of autoinhibition and activation of c-Abl.Computational and structural biotechnology journal · 2022Article
- Synergy and Antagonism between Allosteric and Active-Site Inhibitors of Abl Tyrosine Kinase.Angewandte Chemie (International ed. in English) · 2021Article
- The Seminiferous Epithelial Cycle of Spermatogenesis: Role of Non-receptor Tyrosine Kinases.Advances in experimental medicine and biology · 2021Article
- Reining in BTK: Interdomain Interactions and Their Importance in the Regulatory Control of BTK.Frontiers in cell and developmental biology · 2021Review
- Conformational states dynamically populated by a kinase determine its function.Science (New York, N.Y.) · 2020Article
- Bcr-Abl Allosteric Inhibitors: Where We Are and Where We Are Going to.Molecules (Basel, Switzerland) · 2020Article
- Domain Organization in Plant Blue-Light Receptor Phototropin2 ofInternational journal of molecular sciences · 2020Review
- Chemical genetics strategy to profile kinase target engagement reveals role of FES in neutrophil phagocytosis.Nature communications · 2020Article
- Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms.Nature communications · 2020Article
- Transcriptome analysis during photostimulated recrudescence reveals distinct patterns of gene regulation in Siberian hamster ovaries†.Biology of reproduction · 2020Article
50 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors.
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Abstract
The SH2 domain of cytoplasmic tyrosine kinases can enhance catalytic activity and substrate recognition, but the molecular mechanisms by which this is achieved are poorly understood. We have solved the structure of the prototypic SH2-kinase unit of the human Fes tyrosine kinase, which appears specialized for positive signaling. In its active conformation, the SH2 domain tightly interacts with the kinase N-terminal lobe and positions the kinase alphaC helix in an active configuration through essential packing and electrostatic interactions. This interaction is stabilized by ligand binding to the SH2 domain. Our data indicate that Fes kinase activation is closely coupled to substrate recognition through cooperative SH2-kinase-substrate interactions. Similarly, we find that the SH2 domain of the active Abl kinase stimulates catalytic activity and substrate phosphorylation through a distinct SH2-kinase interface. Thus, the SH2 and catalytic domains of active Fes and Abl pro-oncogenic kinases form integrated structures essential for effective tyrosine kinase signaling.
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