The type I interferon receptor: structure, function, and evolution of a family business.
Recent results indicate that coherent models of how multiple interferons (IFN) are recognized and signal selectively through a common receptor are now feasible. A proposal is made that the IFN receptor, with its subunits IFNAR-1 and IFNAR-2, presents two separate ligand binding sites, and this double structure is both necessary and sufficient to ensure that the different IFN are recognized and can act selectively. The key feature is the duplication of the extracellular domain of the IFNAR-1 subunit and the configurational geometry that this imposes on the intracellular domains of the receptor subunits and their associated tyrosine kinases.
Mogensen
K E
KE
CNRS-EP2030, Montpellier, France.
Lewerenz
M
M
Reboul
J
J
Lutfalla
G
G
Uzé
G
G
D000595:Amino Acid Sequence; D006801:Humans; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D053633:Receptor, Interferon alpha-beta; D017471:Receptors, Interferon / Q000737:chemistry* / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000502:physiology; D013329:Structure-Activity Relationship
C507964:IFNAR1 protein, human; D008565:Membrane Proteins; D017471:Receptors, Interferon; D053633:Receptor, Interferon alpha-beta; D011505:Protein-Tyrosine Kinases