JAK1 binding box domain found in interferon lambda receptor 1 (IFNLR1) and similar proteins
IFNLR1, also called IFN-lambda receptor 1, IFN-lambda-R1, cytokine receptor class-II member 12, cytokine receptor family 2 member 12, CRF2-12, interleukin-28 receptor subunit alpha, IL-28 receptor subunit alpha, IL-28R-alpha, IL-28RA, likely interleukin, or cytokine receptor 2 (LICR2), is a class II cytokine receptor that, together with IL10RB, forms a dimer. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulates the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG) which contribute to the antiviral state. IFNLR1 determines the cell type specificity of the lambda interferon action. It plays a significant role in the antiviral immune defense in the intestinal epithelium. This model corresponds to IFNLR1 box domain which consists of box1 and box2. Mutations within the box1 and box2 motifs disrupt Janus kinase (JAK) binding as well as signaling.
Feature 1:JAK1 binding site [polypeptide binding site]
Evidence:
Comment:Both, box1 and box2, are involved in interactions with JAK1; some structure evidence is obtained from another structure of truncated IFNLR1 bound to JAK1
Jiyao W et al.(2023). "The conserved domain database in 2023.",