What the research shows
Investigators obtained an X-ray crystal structure of GW-0742 bound to the ligand-binding domain of human PPAR-delta. By comparing related structures and changing individual amino acids, they identified two positions in the binding pocket that help explain selectivity. Their result describes the fit between a compound and a protein domain. The structure helps explain molecular selectivity. Human performance and metabolic outcomes require studies in people. Crystal structure and mutation study of the GW-0742 binding pocket.
Documented formats
The crystallography study used the chemical ligand and a purified receptor domain produced for the experiment. The deposited structure is PDB entry 3TKM.
Testing and purity
Match the complete chemical structure to the reported ligand. Other PPAR-delta agonists, including GW501516, have different structures. A target name on its own identifies the receptor but leaves the compound ambiguous.
How to read a batch reportQuestions about GW-0742
What does selectivity describe here?
It describes how strongly the compound favors particular related receptors under the test conditions. Effects in an organism depend on factors such as tissue exposure as well as receptor binding.
What does 3TKM identify?
It identifies the deposited three-dimensional receptor–ligand structure. It allows readers to inspect the binding contacts. The specific compound lot has its own identifier in a laboratory report.