3DGC
Structure of IL-22/IL-22R1
Summary for 3DGC
| Entry DOI | 10.2210/pdb3dgc/pdb |
| Descriptor | Interleukin-22, Interleukin-22 receptor subunit alpha-1, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | il-22, il-22r1, cytokine, receptor, signaling molecule, glycoprotein, secreted, membrane, transmembrane, cytokine-signaling protein complex, cytokine/signaling protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Secreted: Q9GZX6 Membrane; Single-pass type I membrane protein: Q9HB22 |
| Total number of polymer chains | 4 |
| Total formula weight | 84609.62 |
| Authors | Jones, B.C.,Logsdon, N.J.,Walter, M.R. (deposition date: 2008-06-13, release date: 2008-07-15, Last modification date: 2024-11-06) |
| Primary citation | Jones, B.C.,Logsdon, N.J.,Walter, M.R. Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain. Structure, 16:1333-1344, 2008 Cited by PubMed Abstract: IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-10R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with an extracellular region of IL-22R1 (sIL-22R1). IL-22R1 also pairs with the IL-20R2 chain to induce IL-20 and IL-24 signaling. To define the molecular basis of these diverse interactions, we have determined the structure of the IL-22/sIL-22R1 complex. The structure, combined with homology modeling and surface plasmon resonance studies, defines the molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses. PubMed: 18599299DOI: 10.1016/j.str.2008.06.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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