金山科研平台，产品价格货期咨询微信：jinshanbio Molecule Information: DDR2 Long Name: Discoidin Domain Receptor 2 Aliases: TKT; Trk3; Tyro-10 Entrez Gene IDs: 4921 (Human); 18214 (Mouse) Background: Discoidin Domain Receptor 2

DDR2 selectively recognizes the triple helical structure of collagen compared to monomeric or denatured collagen. Within collagen II, the D2 period is required for DDR2 binding, and the D1 period is additionally required to trigger DDR2 auto-phosphorylation. The ECD of DDR2 exists as a noncovalent dimer in solution, and dimerization of the receptor greatly enhances collagen binding. DDR2 interaction with collagen I inhibits collagen fibrillogenesis and alters collagen fiber morphology. Ligand binding induces DDR2 auto-phosphorylation in the cytoplasmic domain, which promotes associations with Shc and Src. In addition to the above mechanism, DDR2 exhibits a distinct interaction with collagen X. A region other than the discoidin-like domain of DDR2 recognizes the non-helical NC1 domain of collagen X, and this interaction does not lead to receptor auto-phosphorylation. Activation of DDR2 by collagen induces upregulation of MMP1, 2, and 13 as well as DDR2 itself. DDR2 is implicated in collagenous matrix destruction and cell invasiveness. DDR2 is also upregulated in several pathological conditions, including hepatic fibrosis following injury, rheumatoid and osteoarthritis, and smooth muscle cell hyperplasia.