Recruitment of IFNAR1

Stable Identifier
Reaction [binding]
Homo sapiens
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The extracellular domain of IFNAR1 is atypical, consisting of a tandem array of four FNIII domains and the first three N-terminal FNIII domains are involved in ligand recognition. IFNAR1 is recruited to the binary complex (IFNA/B:IFNAR2) on the membrane to form the ternary complex (IFNAR2:IFNA/B:IFNAR1). TYK2 kinase is pre-associated with IFNAR1 and JAK1 with IFNAR2. The binding of IFNA/B to IFNA receptors brings these JAK kinase together, allowing cross-phosphorylation and kinase activation.

Literature References
PubMed ID Title Journal Year
16171819 Mutational analysis of the IFNAR1 binding site on IFNalpha2 reveals the architecture of a weak ligand-receptor binding-site

Jaitin, DA, Schreiber, G, Roisman, LC, Baker, DP

J Mol Biol 2005
15449939 Identification of residues of the IFNAR1 chain of the type I human interferon receptor critical for ligand binding and biological activity

Sempé, P, Gallet, X, Nardeux, PC, Guymarho, J, Eid, P, Tovey, MG, Cajean-Feroldi, C, Escary, JL, Nosal, F, Baychelier, F

Biochemistry 2004
17969444 The receptor of the type I interferon family

Pellegrini, S, Piehler, J, Schreiber, G, Uzé, G

Curr Top Microbiol Immunol 2007
15312780 Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers

Piehler, J, Gavutis, M, Lata, S, Lamken, P

J Mol Biol 2004
This event is regulated