| Fibroblast Growth Factor Receptor |
Article Index for Fibroblast Growth |
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Information AboutFibroblast Growth Factor Receptor |
| CATEGORIES ABOUT FIBROBLAST GROWTH FACTOR RECEPTOR | |
| tyrosine kinase receptors | |
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STRUCTURE The Fibroblast Growth Factor receptors consist of an extracellular Ligand domain comprised of three Immunoglobulin -like domains, a single transmembrane Helix domain, and an Intracellular domain with Tyrosine Kinase activity. The Fibroblast Growth Factor s are the largest family of growth factor ligands comprising of 23 members.1 The natural Alternate Splicing of four fibroblast growth factor receptor (FRFR) genes results in the production of over 48 different Isoform s of FGFR.2 These isoforms vary in their ligand binding properties and kinase domains, however all share the common extracellular region composed of three Immunoglobulin (Ig) like domains (D1-D3), and thus belong to the Immunoglobulin Superfamily .3 The three immunoglobin(Ig)-like domains, D1, D2 and D3, present a stretch of Acid ic Amino Acid s ("the acidic box") between D1 and D2. This "acidic box" can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. Each receptor can be activated by several FGFs. In many cases the FGFs themselves can also activate more than one receptor, this is not the case with FGF-7 however which can only activate FGFR2b. A gene for a fifth FGFR protein, FGFR5, has also been identified. In contrast to FGFRs 1-4 it lacks a cytoplasmic tyrosine kinase domain and one isoform, FGFR5γ, only contains the extracellular domains D1 and D2.4 The FGFRs are known to Dimer ize as Heterodimer s and homodimers. GENES So far, five distinct membrane FGFR have been identified in Vertebrate s and all of them belong to the Tyrosine Kinase superfamily (FGFR1 to FGFR4).
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