Discoidin domain-containing receptor tyrosine kinase 2 (DDR2)

Discoidin domain-containing receptor tyrosine kinase 2 (DDR2) is a member of the receptor tyrosine kinase family uniquely activated by binding fibrillar collagens rather than soluble growth factors. It contains an extracellular discoidin homology domain that mediates collagen binding. Upon ligand engagement—primarily with type I, III, and X collagens—DDR2 undergoes autophosphorylation on intracellular domains leading to activation of downstream signaling cascades that regulate cellular differentiation, proliferation, migration, adhesion dynamics with the ECM, and tissue remodeling. Aberrant activation or mutation of DDR2 has been implicated in various pathological conditions including cancer progression/metastasis and fibrotic diseases[1][3][6].

Other names

CD167bDDR2Discoidin domain receptor 2

Drugs targeting DDR2 typically act as ATP-binding site inhibitors that block its tyrosine kinase activity, thereby inhibiting downstream signaling pathways involved in cell proliferation, migration, and ECM remodeling[8].