3DLQ

Crystal structure of the IL-22/IL-22R1 complex

Summary for 3DLQ

• Entry DOI: 10.2210/pdb3dlq/pdb
• Descriptor: Interleukin-22, Interleukin-22 receptor subunit alpha-1 (3 entities in total)
• Functional Keywords: cytokine-receptor complex, fibronectin-iii, cytokine, glycoprotein, polymorphism, secreted, membrane, receptor, transmembrane, cytokine-cytokine receptor complex, cytokine/cytokine receptor
• Biological source: Homo sapiens (Human); More
• Cellular location: Secreted: Q9GZX6; Membrane; Single-pass type I membrane protein: Q8N6P7
• Total number of polymer chains: 2
• Total formula weight: 41278.04

Authors

Bleicher, L.,de Moura, P.R.,Watanabe, L.,Colau, D.,Dumoutier, L.,Renauld, J.-C.,Polikarpov, I. (deposition date: 2008-06-28, release date: 2008-08-19, Last modification date: 2024-10-30)

Primary citation

Bleicher, L.,de Moura, P.R.,Watanabe, L.,Colau, D.,Dumoutier, L.,Renauld, J.-C.,Polikarpov, I.
Crystal structure of the IL-22/IL-22R1 complex and its implications for the IL-22 signaling mechanism
Febs Lett., 582:2985-2992, 2008

PubMed Abstract: Interleukin-22 (IL-22) is a member of the interleukin-10 cytokine family, which is involved in anti-microbial defenses, tissue damage protection and repair, and acute phase responses. Its signaling mechanism involves the sequential binding of IL-22 to interleukin-22 receptor 1 (IL-22R1), and of this dimer to interleukin-10 receptor 2 (IL-10R2) extracellular domain. We report a 1.9A crystal structure of the IL-22/IL-22R1 complex, revealing crucial interacting residues at the IL-22/IL-22R1 interface. Functional importance of key residues was confirmed by site-directed mutagenesis and functional studies. Based on the X-ray structure of the binary complex, we discuss a molecular basis of the IL-22/IL-22R1 recognition by IL-10R2.

PubMed: 18675809
DOI: 10.1016/j.febslet.2008.07.046

Experimental method

X-RAY DIFFRACTION (1.9 Å)