|
|||||
|
|
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22 |
|
| Authors: | Patricia Ribeiro de Moura Lucas Bleicher Laure Dumoutier Muriel M Lemaire Jean-Christophe Renauld Igor Polikarpov |
| Institution: | a Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos 13560-970, SP, Brazil b Ludwig Institute for Cancer Research, Brussels Branch, Belgium c Experimental Medicine Unit, Christian de Duve Institute, Université Catholique de Louvain, Brussels, Belgium |
| Abstract: | 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 2.75 Å 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) |
| Keywords: | IL-22BP interleukin-22 binding protein IL-22 interleukin-22 IL-22R1 interleukin-22 receptor 1 IL-10R2 interleukin-10 receptor 2 IL-10 interleukin 10 CRF2-9 cytokine receptor family class 2 member 9 CRF2-4 the second chain of the IL-10 receptor complex CFR2-10 cytokine receptor family class 2 member 10 IL-22Rα2 IL-22 receptor subunit alpha-2 ORF open reading frame PDGF-R platelet-derived growth factor receptor FACS fluorescent automatic cell sorter FITC fluorescein isothiocyanate r m s d root mean square deviation IL-10R1 interleukin-10 receptor 1 FBN-III fibronectin-III domain |
| 本文献已被 ScienceDirect 等数据库收录！ | |