Fibroblast growth factor receptor kinase (FGFR kinase)

Fibroblast growth factor receptor kinases are a subfamily of receptor tyrosine kinases that mediate cellular responses to fibroblast growth factors. There are four main human isoforms—FGFR1, FGFR2, FGFR3, and FGFR4—each consisting of an extracellular ligand-binding domain, a single transmembrane helix, and an intracellular split tyrosine kinase domain. Upon binding their FGF ligands at the cell surface, these receptors dimerize and undergo trans-autophosphorylation on key intracellular tyrosines within their activation loop (notably Y653/Y654 in FGFR1), which dramatically increases catalytic activity and initiates downstream signaling cascades involved in cell proliferation, differentiation, metabolism regulation, embryonic development, tissue repair and homeostasis[2][3]. Dysregulation through activating mutations or overexpression is implicated in various cancers as well as developmental syndromes. The structural features of their active/inactive states have enabled structure-based drug design for selective inhibitors targeting disease-causing forms; however selectivity remains challenging due to high homology among protein kinases[1][4]. Note: The term "FGF kinases" is not standard nomenclature. The correct canonical form should be "Fibroblast growth factor receptor kinase" or more specifically one of its isoforms such as "Fibroblast growth factor receptor 1". Therefore, is_incorrect = true because "FGF kinases" is ambiguous—it could refer either to fibroblast growth factors themselves (which are ligands) or more accurately to their receptors' intracellular kinase domains. For structured data purposes use “Fibroblast growth factor receptor” with specification if possible. If you need information about a specific member such as “Fibroblast growth factor receptor 1”, please specify further for greater accuracy.

Other names

Fibroblast growth factor receptorFGFRFGF receptor tyrosine kinaseFGFR1/2/3/4 (for specific isoforms)

Inhibition of ATP binding to the kinase domain, blocking autophosphorylation and downstream signaling.