Difference between revisions of "Part:BBa K3934000"

<span> Fibroblast growth factor 2 (FGF2) is one of 19 known members of the mammalian FGF family, involved in morphogenesis, development, angiogenesis and wound healing (Plotnikov 2020). It is a mitogen and was first isolated in 1974, from the bovine pituitary and in 1988 human FGF2 was described for the first time (Benington 2020). There are four different FGF receptor tyrosine kinases, to which FGFs bind and induce cell signaling. FGF2 binds FGFR1 and FGFR2 to induce proliferation (Lim 2016). FGFR2 consists of an extracellular domain, a transmembrane helix, and a catalytic intracellular tyrosine kinase domain (Plotnikov 2020). The extracellular domain of the receptor consists of three immunoglobulin-like domains. FGF2 binds to domain 2 (D2) and domain 3 (D3), and the linker region connects the two domains (Plotnikov 2020) (figure x).