ArticleStructure (London, England : 1993)2013
Structural mimicry of a-loop tyrosine phosphorylation by a pathogenic FGF receptor 3 mutation.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
- Substrate-Derived Peptides for Selective Covalent Inhibition of Protein Tyrosine Kinases.ACS chemical biology · 2026Article
- Sequencing of Fibroblast Growth Factor Receptor Inhibitors in Cholangiocarcinoma: A Review of Published Cases.JCO precision oncology · 2026Review
- Substrate-derived peptides for selective covalent inhibition of protein tyrosine kinases.bioRxiv : the preprint server for biology · 2026Article
- Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Warburg-Cinotti disease variant p.Tyr740Cys enhances catalytic activity of DDR2 kinase.PloS one · 2025Article
- Exploring the Micro-Mosaic Landscape ofGenes · 2024Article
- The combined action of the intracellular regions regulates FGFR2 kinase activity.Communications biology · 2023Article
- Measurement of FGFR3 signaling at the cell membrane via total internal reflection fluorescence microscopy to compare the activation of FGFR3 mutants.The Journal of biological chemistry · 2023Article
- Progress toward automated methyl assignments for methyl-TROSY applications.Structure (London, England : 1993) · 2022Article
- FGFR3 overexpression is a useful detection tool for FGFR3 fusions and sequence variations in glioma.Neuro-oncology practice · 2021Article
- Molecular basis for receptor tyrosine kinase A-loop tyrosine transphosphorylation.Nature chemical biology · 2020Article
- A Conserved Allosteric Pathway in Tyrosine Kinase Regulation.Structure (London, England : 1993) · 2019Article
- Structure, activation and dysregulation of fibroblast growth factor receptor kinases: perspectives for clinical targeting.Biochemical Society transactions · 2018Review
- NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 3 in apo state and in complex with inhibitor PD173074.Biomolecular NMR assignments · 2018Article
- Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.Structure (London, England : 1993) · 2018Article
- A threshold model for receptor tyrosine kinase signaling specificity and cell fate determination.F1000Research · 2018Review
- Polyclonal SecondaryCancer discovery · 2017Article
- Elucidation of a four-site allosteric network in fibroblast growth factor receptor tyrosine kinases.eLife · 2017Article
- Effects of FGFR2 kinase activation loop dynamics on catalytic activity.PLoS computational biology · 2017Article
- KinView: a visual comparative sequence analysis tool for integrated kinome research.Molecular bioSystems · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The K650E gain-of-function mutation in the tyrosine kinase domain of FGF receptor 3 (FGFR3) causes Thanatophoric Dysplasia type II, a neonatal lethal congenital dwarfism syndrome, and when acquired somatically, it contributes to carcinogenesis. In this report, we determine the crystal structure of the FGFR3 kinase domain harboring this pathogenic mutation and show that the mutation introduces a network of intramolecular hydrogen bonds to stabilize the active-state conformation. In the crystal, the mutant FGFR3 kinases are caught in the act of trans-phosphorylation on a kinase insert autophosphorylation site, emphasizing the fact that the K650E mutation circumvents the requirement for A-loop tyrosine phosphorylation in kinase activation. Analysis of this trans-phosphorylation complex sheds light onto the determinants of tyrosine trans-phosphorylation specificity. We propose that the targeted inhibition of this pathogenic FGFR3 kinase may be achievable by small molecule kinase inhibitors that selectively bind the active-state conformation of FGFR3 kinase.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.