The type I interferon receptor: Structure, function, and evolution of a family business

Recent results indicate that coherent models of how multiple interferons (I FN) are recognized and signal selectively through a common receptor are now feasible, A proposal is made that the IFN receptor, with its subunits IFNA R-1 and IFNAR-2, presents two separate ligand binding sites, and this doubl e structure is both necessary and sufficient to ensure that the different I FN are recognized and can act selectively. The key feature is the duplicati on of the extracellular domain of the IFNAR-1 subunit and the configuration al geometry that this imposes on the intracellular domains of the receptor subunits and their associated tyrosine kinases.