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3DGC

Structure of IL-22/IL-22R1

Summary for 3DGC
Entry DOI10.2210/pdb3dgc/pdb
DescriptorInterleukin-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 Keywordsil-22, il-22r1, cytokine, receptor, signaling molecule, glycoprotein, secreted, membrane, transmembrane, cytokine-signaling protein complex, cytokine/signaling protein
Biological sourceHomo sapiens (human)
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Cellular locationSecreted: Q9GZX6
Membrane; Single-pass type I membrane protein: Q9HB22
Total number of polymer chains4
Total formula weight84609.62
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 citationJones, 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: 18599299
DOI: 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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