Discoidin domain receptors (DDRs) are members of the transmembrane receptor tyrosine kinase (RTK) superfamily which are distinguished from others by the presence of a discoidin motif in the extracellular domain and their utilization of collagens as internal ligands. DDR1 and DDR2, two types of DDRs with different expression patterns and ligand preferences, have been discovered.
DDRs bind to collagen and then transmit cellular signaling that is involved in a number of different cell processes, such as adhesion, proliferation, differentiation, migration, and matrix homeostasis. Atherosclerosis, inflammation, cancer, and tissue fibrosis have all been linked to altered DDR function that results from either mutations or overexpression. New small molecule inhibitors that target the receptors are being sought after because DDRs have been identified as novel potential molecular targets for drug discovery.
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