Proteins in the tumor necrosis factor (TNF) superfamily (TNFSF) regulate
diverse cellular processes by interacting with their receptors in the
TNF receptor (TNFR) superfamily (TNFRSF). Ligands and receptors in these
two superfamilies form a complicated network of interactions, in which
the same ligand can bind to different receptors and the same receptor
can be shared by different ligands. In order to study these interactions
on a systematic level, a TNFSF-TNFRSF interactome was constructed in
this study by searching the database which consists of both
experimentally measured and computationally predicted protein-protein
interactions (PPIs). The interactome contains a total number of 194
interactions between 18 TNFSF ligands and 29 TNFRSF receptors in human.
We modeled the structure for each ligand-receptor interaction in the
network. Their binding affinities were further computationally estimated
based on modeled structures. Our computational outputs, which are all
publicly accessible, serve as a valuable addition to the currently
limited experimental resources to study TNF-mediated cell signaling.