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Su, Zhaoqian; Wu, Yinghao
Computational and structural biotechnology journal, 01/2020, Volume: 18Journal Article
Display omitted By recognizing members in the tumor necrosis factor (TNF) receptor superfamily, TNF ligand proteins function as extracellular cytokines to activate various signaling pathways involved in inflammation, proliferation, and apoptosis. Most ligands in TNF superfamily are trimeric and can simultaneously bind to three receptors on cell surfaces. It has been experimentally observed that the formation of these molecular complexes further triggers the oligomerization of TNF receptors, which in turn regulate the intracellular signaling processes by providing transient compartmentalization in the membrane proximal regions of cytoplasm. In order to decode the molecular mechanisms of oligomerization in TNF receptor superfamily, we developed a new computational method that can physically simulate the spatial-temporal process of binding between TNF ligands and their receptors. The simulations show that the TNF receptors can be organized into hexagonal oligomers. The formation of this spatial pattern is highly dependent not only on the molecular properties such as the affinities of trans and cis binding, but also on the cellular factors such as the concentration of TNF ligands in the extracellular area or the density of TNF receptors on cell surfaces. Moreover, our model suggests that if TNF receptors are pre-organized into dimers before ligand binding, these lateral interactions between receptor monomers can play a positive role in stabilizing the ligand-receptor interactions, as well as in regulating the kinetics of receptor oligomerization. Altogether, this method throws lights on the mechanisms of TNF ligand-receptor interactions in cellular environments.
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