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

Author(s)

de Moura, Patricia Ribeiro ; Watanabe, Leandra ; Bleicher, Lucas ; Colau, Didier ; Dumoutier, Laure ; Lemaire, Muriel M. ; Renauld, Jean-Christophe ; Polikarpov, Igor

• Document type: Journal article
• Source: FEBS LETTERS; v. 583, n. 7, p. 6-pg., 2009-04-02.

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