Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
Autor: | Patricia Ribeiro de Moura, Igor Polikarpov, Laure Dumoutier, Didier Colau, Muriel M. Lemaire, Lucas Bleicher, Jean-Christophe Renauld, Leandra Watanabe |
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Rok vydání: | 2009 |
Předmět: |
Immunology
Biophysics Plasma protein binding Biochemistry Structural Biology Genetics IL-22 Humans 5-HT5A receptor Binding site Receptor Protein Structure Quaternary Molecular Biology Cytokine X-ray crystallography Inflammation Binding Sites biology Binding protein Interleukins SISTEMA IMUNE Biological activity Cell Biology Receptors Interleukin Interleukin Interleukin-10 Receptor beta Subunit Molecular biology Cell biology Interleukin 10 IL-22BP biology.protein Mutagenesis Site-Directed Platelet-derived growth factor receptor Protein Binding |
Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
Popis: | Interleukin-22 (IL-22) plays an important role in the regulation of immune and inflammatory responses in mammals. The IL-22 binding protein (IL-22BP), a soluble receptor that specifically binds IL-22, prevents the IL-22/interleukin-22 receptor 1 (IL-22R1)/interleukin-10 receptor 2 (IL-10R2) complex assembly and blocks IL-22 biological activity. Here we present the crystal structure of the IL-22/IL-22BP complex at 2.75Å resolution. The structure reveals IL-22BP residues critical for IL-22 binding, which were confirmed by site-directed mutagenesis and functional studies. Comparison of IL-22/IL-22BP and IL-22/IL-22R1 crystal structures shows that both receptors display an overlapping IL-22 binding surface, which is consistent with the inhibitory role played by IL-22 binding protein.Structured summaryMINT-7010533: IL-22 BP (uniprotkb:Q969J5) and IL-22 (uniprotkb:Q9GZX6) bind (MI:0407) by X-ray crystallography (MI:0114) |
Databáze: | OpenAIRE |
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