3KY2
Crystal structure of Fibroblast Growth Factor Receptor 1 kinase domain
Summary for 3KY2
| Entry DOI | 10.2210/pdb3ky2/pdb |
| Related | 3KXX |
| Descriptor | Basic fibroblast growth factor receptor 1, SULFATE ION (3 entities in total) |
| Functional Keywords | kinase, rtk, phosphorylation, interface, alternative splicing, atp-binding, chromosomal rearrangement, craniosynostosis, disease mutation, disulfide bond, dwarfism, glycoprotein, heparin-binding, hypogonadotropic hypogonadism, immunoglobulin domain, kallmann syndrome, membrane, nucleotide-binding, phosphoprotein, polymorphism, receptor, transferase, transmembrane, tyrosine-protein kinase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 72837.46 |
| Authors | Bae, J.H.,Boggon, T.J.,Tome, F.,Mandiyan, V.,Lax, I.,Schlessinger, J. (deposition date: 2009-12-04, release date: 2010-03-02, Last modification date: 2023-09-06) |
| Primary citation | Bae, J.H.,Boggon, T.J.,Tome, F.,Mandiyan, V.,Lax, I.,Schlessinger, J. Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells. Proc.Natl.Acad.Sci.USA, 107:2866-2871, 2010 Cited by PubMed Abstract: Tyrosine autophosphorylation of receptor tyrosine kinases plays a critical role in regulation of kinase activity and in recruitment and activation of intracellular signaling pathways. Autophosphorylation is mediated by a sequential and precisely ordered intermolecular (trans) reaction. In this report we present structural and biochemical experiments demonstrating that formation of an asymmetric dimer between activated FGFR1 kinase domains is required for transphosphorylation of FGFR1 in FGF-stimulated cells. Transphosphorylation is mediated by specific asymmetric contacts between the N-lobe of one kinase molecule, which serves as an active enzyme, and specific docking sites on the C-lobe of a second kinase molecule, which serves a substrate. Pathological loss-of-function mutations or oncogenic activating mutations in this interface may hinder or facilitate asymmetric dimer formation and transphosphorylation, respectively. The experiments presented in this report provide the molecular basis underlying the control of transphosphorylation of FGF receptors and other receptor tyrosine kinases. PubMed: 20133753DOI: 10.1073/pnas.0914157107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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