3lqm
From Proteopedia
Structure of the IL-10R2 Common Chain
Structural highlights
Disease[I10R2_HUMAN] Autosomal recessive early-onset inflammatory bowel disease. The disease is caused by mutations affecting the gene represented in this entry. Function[I10R2_HUMAN] Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIL-10R2 is a shared cell surface receptor required for the activation of five class 2 cytokines (IL-10, IL-22, IL-26, IL-28, and IL-29) that play critical roles in host defense. To define the molecular mechanisms that regulate its promiscuous binding, we have determined the crystal structure of the IL-10R2 ectodomain at 2.14 A resolution. IL-10R2 residues required for binding were identified by alanine scanning and used to derive computational models of IL-10/IL-10R1/IL-10R2 and IL-22/IL-22R1/IL-10R2 ternary complexes. The models reveal a conserved binding epitope that is surrounded by two clefts that accommodate the structural and chemical diversity of the cytokines. These results provide a structural framework for interpreting IL-10R2 single nucleotide polymorphisms associated with human disease. Structure and mechanism of receptor sharing by the IL-10R2 common chain.,Yoon SI, Jones BC, Logsdon NJ, Harris BD, Deshpande A, Radaeva S, Halloran BA, Gao B, Walter MR Structure. 2010 May 12;18(5):638-48. PMID:20462497[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Human | Walter, M R | Yoon, S I | Common chain | Cytokine | Disulfide bond | Glycoprotein | Il-10 | Il-10r2 | Il-22 | Il-26 | Il-28 | Il-29 | Membrane | Phosphoprotein | Polymorphism | Protein binding | Receptor | Transmembrane
