Discoidin Domain Receptor 2 (DDR2) Also known as CD167 antigen-like family member B (CD167b), Discoidin domain receptor tyrosine kinase 2, neurotrophic tyrosine kinase, receptor-associated 3 (NTRKR3), tyrosine protein kinase TYRO10. The receptor encoded by this gene belongs to the tyrosine kinase (RTKs) protein family. RTKs play a key role in the communication between cells and their microenvironment. As a cell surface receptor for fibrillar collagen, DDR2 can regulate cell differentiation, extracellular matrix remodeling, cell migration, and cell proliferation. Research shows that DDR2 is required for normal bone development. DDR2 regulates osteoblast differentiation and chondrocyte maturation through signaling pathways involving MAP kinases and leads to activation of the transcription factor RUNX2. Further studies found that DDR2 protein is expressed in multiple cell types and may also be involved in wound repair and short-limbed hand-type spondyloepiphyseal dysplasia. In addition, DDR2 regulates extracellular matrix remodeling by upregulating collagenases MMP1, MMP2, and MMP13, thereby promoting cell migration and tumor cell invasion. Therefore, it is a marketable option to develop tumor therapeutic drugs targeting DDR2. CD ComputaBio provides DDR2 targeting services to customers to accelerate the progress of their research.
Our Services
- Targeted protein structural analysis
The crystal structure of the DDR2 protein molecule can be simulated by X-ray single crystal diffraction technology or the 3D structure of the existing homologous molecule, and then the information of its binding site can be determined through structural analysis;
- Analysis of target protein properties
We can use molecular simulation software to analyze the structural characteristics of the DDR2 binding site, such as electrostatic field, hydrophobic field, and distribution of hydrogen bonding sites;
- Lead Candidate Search
After obtaining the binding site information, use database search software or new drug molecular design technology to screen molecules whose molecular morphology and physicochemical properties match the DDR2 action site;
- Candidate compound validation
Finally, we synthesize and test the screened molecules, and after multiple rounds of screening, suitable lead compounds can be found.
Our Advantage
- Our experts can quickly and accurately find atoms or groups that interact well with the active site of biological macromolecules through active site analysis software such as DRID, GREEN, HSITE, combined with Monte Carlo and simulated annealing techniques;
- Flexible selection of ligand-based (commonly used software such as Catalyst and Unity, etc.) and receptor-based (commonly used software such as DOCK, F1exX and GOLD, etc.) search methods for database search;
- In the event that a suitable lead compound cannot be found in the compound database, we offer a new compound synthesis service, which enables new compound design through advanced bioinformatics software.
Our Capabilities
In each therapeutic area, CD ComputaBio has accumulated deep expertise in discovery informatics, computational chemistry/molecular modeling, medicinal chemistry, structural biology, in vivo and in vitro pharmacology, and translational science. During the drug discovery process, our team focuses on early lead compounds in different target classes and uses a wide range of techniques, including molecular screening, molecular modeling, medicinal chemistry, structural biology, bioinformatics and computational chemistry, to identify new target the direction of drug development, and then select suitable drug candidates through low-cost, high-efficiency computer simulations to ensure high efficiency and low risk in the later drug development process. Our computational biology team has extensive experience in the research of DDR2 targets. Please consult our professional team for details.
References
- Fu HL, et al.; Discoidin domain receptors: unique receptor tyrosine kinases in collagen-mediated signaling. J. Biol. Chem. 2013, 288 (11): 7430–7.
- Iwai LK, et al.; Phosphoproteomics of collagen receptor networks reveals SHP-2 phosphorylation downstream of wild-type DDR2 and its lung cancer mutants. Biochem. J. 2013, 454 (3): 501–13.
* For Research Use Only.
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