BCHM 210 Midterm: Growth Factor Receptors
Document Summary
Egf it can stimulate the growth of cells (epidermal and epithelial cells) It is stabilized via 3 disulfide bonds; the structure is preserved by having these 3 disulfide bonds: egf activates a tyrosine kinase receptor 2 molecules of egf bind to the receptor. This egf receptor has a egf binding domain, a transmembrane helix and a kinase domain and lastly a c-terminal tail that is tyrosine rich. Unlike those of the insulin receptor, however, these units exist as monomers until they bind egf. Moreover, each egf receptor monomer binds a single molecule of egf in its extracellular domain. Thus the dimer binds two ligand molecules, in contrast with the insulin-receptor dimer, which binds only one ligand. Note that each egf molecule lies far away from the dimer interface. This interface includes a so-called dimerization arm from each monomer that reaches out and inserts into a binding pocket on the other monomer.
