Structural Characterization of Tumor Necrosis Factor Ligand TL1A and Food Allergens

The method of X-ray Crystallography was used to study to the crystal structure of human tumor necrosis factor TL1A and food allergens. TL1A forms a homotrimer with each monomer assuming a jellyroll beta-sandwich fold. With the experimentally determined structure of TL1A, a TL1A-DR3 complex model was built by homology modeling and protein docking calculations. This TL1A-DR3 interaction model can be used in designing novel therapeutical reagents by modulating the TL1A-DR3 signaling pathways. In addition, a protocol for preparing functional TL1A protein from inactive inclusion bodies is described. The cost-effective refolding procedure may be used for large scale production of this highly promising candidate as a therapeutical reagent for research use. The seed proteins from pine nut, peanut, almond, ginkgo, and bitter melon were isolated and their biochemical properties and structures were studied. The characterization of these proteins enriches the understanding of food induced allergy.