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3G9V

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

Summary for 3G9V
Entry DOI10.2210/pdb3g9v/pdb
DescriptorInterleukin 22 receptor, alpha 2, Interleukin-22 (3 entities in total)
Functional Keywordscytokine, cytokine receptor, receptor, glycoprotein, polymorphism, secreted, cytokine-cytokine receptor complex, cytokine/cytokine receptor
Biological sourceHomo sapiens (Human)
More
Cellular locationSecreted: Q9GZX6
Total number of polymer chains4
Total formula weight83842.87
Authors
de Moura, P.R.,Watanabe, L.,Bleicher, L.,Colau, D.,Renauld, J.-C.,Polikarpov, I. (deposition date: 2009-02-14, release date: 2009-04-14, Last modification date: 2024-10-30)
Primary citationde Moura, P.R.,Watanabe, L.,Bleicher, L.,Colau, D.,Dumoutier, L.,Lemaire, M.M.,Renauld, J.-C.,Polikarpov, I.
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
FEBS Lett., 583:1072-1077, 2009
Cited by
PubMed 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 A 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.
PubMed: 19285080
DOI: 10.1016/j.febslet.2009.03.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.756 Å)
Structure validation

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