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Fibroblast growth factor receptor 1 (FGFR1) and fibroblast growth factor receptor 2 (FGFR2) are cell-surface tyrosine-protein kinases that act as high-affinity receptors for fibroblast growth factors (FGFs). Structurally, each consists of three extracellular immunoglobulin-like domains (D1-D3), a single transmembrane helix, and an intracellular split tyrosine kinase domain. Ligand binding triggers receptor dimerization and activation of kinase activity, leading to pathways that control cell proliferation, differentiation, migration, and survival. FGFR1/2 play central roles in embryonic development, tissue homeostasis, angiogenesis, and wound repair. Genetic alterations of FGFR1/2 can drive cancers, skeletal disorders, and other diseases, making them prominent drug targets in oncology and regenerative medicine.
Inhibition of kinase activity (blocking phosphorylation and downstream signal transduction); Disruption of ligand binding; Receptor dimerization blockade
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