DDR1
DDR1
DDR1, also known as Discoidin Domain Receptor Tyrosine Kinase 1, is a type of protein encoded by the DDR1 gene in humans. It is a member of a novel subfamily of tyrosine kinase receptors with an extracellular domain homologous to Dictyostelium discoideum protein discoidin I in their extracellular region. The DDR1 protein is a receptor for collagen and plays a crucial role in various biological processes.
Structure
The DDR1 protein is a transmembrane receptor that is activated by collagen binding. It consists of a large extracellular region, a single transmembrane region, and a cytoplasmic region. The extracellular region contains a discoidin domain, which is responsible for binding to collagen. The cytoplasmic region contains a tyrosine kinase domain, which is responsible for the protein's enzymatic activity.
Function
DDR1 is involved in various cellular functions, including cell adhesion, cell migration, proliferation, and differentiation. It plays a crucial role in tissue repair, primarily through its involvement in the regulation of cell-matrix interactions. In addition, DDR1 has been implicated in the pathogenesis of several diseases, including cancer, fibrosis, and atherosclerosis.
Clinical significance
Alterations in the DDR1 gene have been associated with several types of cancer, including breast cancer, lung cancer, and brain cancer. Overexpression of DDR1 has been observed in many cancer types, suggesting that it may play a role in tumor progression. In addition, DDR1 has been implicated in the development of fibrosis, a condition characterized by excessive deposition of collagen in tissues.
Research
Research on DDR1 has focused on understanding its role in disease and developing targeted therapies. Several small molecule inhibitors of DDR1 have been developed and are currently being tested in preclinical studies. These inhibitors have the potential to be used as targeted therapies for diseases associated with DDR1 overexpression or mutation.
See also
References
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