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Expression, purification and crystallization of recombinant human TRAIL.
1Department of Life Science and School of Environmental Engineering, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, South Korea.
Summary
Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) triggers apoptosis in cancer cells but not normal cells. Researchers crystallized TRAIL to determine its structure and mechanism of action.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces apoptosis in tumor cells via death receptors.
- Normal cells resist TRAIL-induced apoptosis through decoy receptors that lack functional death domains.
Purpose of the Study:
- To determine the crystal structure of soluble and functional human TRAIL.
- To elucidate the structural basis for TRAIL's selective apoptosis induction.
Main Methods:
- Expression and refolding of soluble human TRAIL in Escherichia coli.
- Crystallization of TRAIL and collection of X-ray diffraction data.
- Structure determination using molecular replacement and isomorphous replacement.
Main Results:
- TRAIL crystals belong to space group P63 with specific unit-cell dimensions.
- The asymmetric unit contains two TRAIL molecules.
- X-ray diffraction data were collected to 2.8-3.5 A resolution.
Conclusions:
- The crystal structure of TRAIL is being determined.
- Understanding TRAIL's structure will aid in developing targeted cancer therapies.
- Structural insights may reveal mechanisms of decoy receptor antagonism.