Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
(2009) FEBS Letters — Vol. 583, n° 7, p. 1072-1077 (2009)
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- 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.
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de Moura, P. R., Watanabe, L., Bleicher, L., Colau, D., Dumoutier, L., Lemaire, M., Renauld, J.-C., & Polikarpov, I. (2009). Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22. FEBS Letters, 583(7), 1072-1077. https://doi.org/10.1016/j.febslet.2009.03.006 (Original work published 2009)