Recruitment of IFNAR1

Stable Identifier
R-HSA-909724
Type
Reaction [binding]
Species
Homo sapiens
Compartment
plasma membrane
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Recruitment of IFNAR1
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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
15449939 Identification of residues of the IFNAR1 chain of the type I human interferon receptor critical for ligand binding and biological activity

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

Biochemistry 2004
16171819 Mutational analysis of the IFNAR1 binding site on IFNalpha2 reveals the architecture of a weak ligand-receptor binding-site

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

J Mol Biol 2005
17969444 The receptor of the type I interferon family

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

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

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

J Mol Biol 2004
Participants
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Output
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Orthologous Events
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Authored
Garapati, P V  (2010-07-07)
Reviewed
Abdul-Sater, AA  (2010-08-17)
Schindler, C  (2010-08-17)
Created
Garapati, P V  (2010-07-07)