Discoidin domain receptor 1 (DDR1) is a member of DDRs, which are members of the receptor tyrosine kinase (RTK). Upon collagen binding, DDR1 undergoes tyrosine autophosphorylation, which consequently triggers downstream genetic and cellular pathways and plays critical roles in the regulation of cellular morphogenesis, differentiation, proliferation, adhesion, migration, and invasion. Research shows that DDR1 is closely related to various human diseases including cancer, fibrosis, atherosclerosis, and other inflammatory disorders. New generation DDR1 inhibitors targeting the allosteric sites outside of the canonical ATP-binding pocket or extracellular domain (allosteric inhibitors) may offer a new opportunity for selective DDR1 inhibition therapy development.