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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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de Moura, Patricia Ribeiro [1] ; Watanabe, Leandra [1] ; Bleicher, Lucas [1] ; Colau, Didier [2] ; Dumoutier, Laure [3, 2] ; Lemaire, Muriel M. [3, 2] ; Renauld, Jean-Christophe [3, 2] ; Polikarpov, Igor [1]
Total Authors: 8
[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
Total Affiliations: 3
Document type: Journal article
Source: FEBS Letters; v. 583, n. 7, p. 1072-1077, APR 2 2009.
Web of Science Citations: 30

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. (AU)

FAPESP's process: 06/00182-8 - Structural biophysics of nuclear receptors and related proteins
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants
FAPESP's process: 06/01534-5 - Studies of the interactions of thyroid hormone receptors with DNA and the coregulator proteins using X-ray crystallography
Grantee:Leandra Watanabe
Support type: Scholarships in Brazil - Post-Doctorate