Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22

被引：70

作者：

de Moura, Patricia Ribeiro ^{[1
]}

Watanabe, Leandra ^{[1
]}

Bleicher, Lucas ^{[1
]}

Colau, Didier ^{[2
]}

Dumoutier, Laure ^{[2
,3
]}

Lemaire, Muriel M. ^{[2
,3
]}

Renauld, Jean-Christophe ^{[2
,3
]}

Polikarpov, Igor ^{[1
]}

机构：

[1] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13560970 Sao Carlos, SP, Brazil

[2] Ludwig Inst Canc Res, Brussels Branch, Brussels, Belgium

[3] Univ Catholique Louvain, Christian Duve Inst, Expt Med Unit, B-1200 Brussels, Belgium

来源：

FEBS LETTERS | 2009年 / 583卷 / 07期

基金：

巴西圣保罗研究基金会;

关键词：

Cytokine; IL-22; IL-22BP; Interleukin; Immunology; X-ray crystallography; T-CELL; INDUCIBLE FACTOR; CYTOKINE; INFLAMMATION; EXPRESSION; IL-10R2; COMPLEX; CLONING; IDENTIFICATION; HEPATOCYTES;

D O I：

10.1016/j.febslet.2009.03.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

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 angstrom 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.

引用

页码：1072 / 1077

页数：6

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