Fibroblast growth factor receptor
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The fibroblast growth factor receptors are, as their name implies, receptors which bind fibroblast growth factor.
[edit] 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 three immunoglobin(Ig)-like domains, namely D1, D2 and D3, present a stretch of acidic amino acids ("the acidic box") between D1 and D2. This "acidic box" can participate to the regulation of FGF binding to the FGFR. Immunoglobulin-like domains II and III are sufficient for FGF binding.
The FGFRs are known to dimerize as heterodimers and homodimers.
[edit] Genes
So far, four distinct membrane FGFR have been identified in vertebrates and all of them belong to the tyrosine kinase superfamily (FGFR1 to FGFR4).
- FGFR1
- FGFR2 (see also Fibroblast growth factor receptor 2)
- FGFR3
- FGFR4
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Angiopoietin Receptors: Tie-1 & Tie-2 - Eph - Epidermal growth factor (HER2/neu, Her 3, Her 4) - Fibroblast growth factor (FGFR2) - Flk-1 Flt-1 Insulin - IGF-1 - MuSK - Platelet-derived growth factor - RET - TRK (TrkA, TrkB, TrkC), VEGF Receptors: Flt-1 & KDR/Flk-1,
