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Receptor tyrosine kinases are transmembrane glycoproteins that are activated by ligand-induced receptor dimerization following by an autophosphorylation of tyrosine residues in the cytoplasmic region and the release of the autoinhibited state of the tyrosine kinase domain. Based on their kinase domain sequence and the overall structure they can be classified into at least five subgroups. The class III RTK's are characterised by the presence of five to seven immunoglobulin-like domains and play an important role in haematopoiesis. Dysregulation of class III RTK's is linked to the pathogenesis of leukemia.
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