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Fibroblast growth factor receptor
From Wikipedia, the free encyclopedia
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This article or section may be confusing or unclear for some readers. Please improve the article or discuss this issue on the talk page. This article has been tagged since January 2007. |
The fibroblast growth factor receptors are, as their name implies, receptors which bind fibroblast growth factor.
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.
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,