3LQM
Structure of the IL-10R2 Common Chain
Summary for 3LQM
| Entry DOI | 10.2210/pdb3lqm/pdb |
| Descriptor | Interleukin-10 receptor subunit beta, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | il-10r2, receptor, common chain, cytokine, il-10, il-22, il-26, il-28, il-29, disulfide bond, glycoprotein, membrane, phosphoprotein, polymorphism, transmembrane, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 48219.45 |
| Authors | Yoon, S.I.,Walter, M.R. (deposition date: 2010-02-09, release date: 2010-05-26, Last modification date: 2024-11-27) |
| Primary citation | Yoon, S.I.,Jones, B.C.,Logsdon, N.J.,Harris, B.D.,Deshpande, A.,Radaeva, S.,Halloran, B.A.,Gao, B.,Walter, M.R. Structure and mechanism of receptor sharing by the IL-10R2 common chain. Structure, 18:638-648, 2010 Cited by PubMed Abstract: IL-10R2 is a shared cell surface receptor required for the activation of five class 2 cytokines (IL-10, IL-22, IL-26, IL-28, and IL-29) that play critical roles in host defense. To define the molecular mechanisms that regulate its promiscuous binding, we have determined the crystal structure of the IL-10R2 ectodomain at 2.14 A resolution. IL-10R2 residues required for binding were identified by alanine scanning and used to derive computational models of IL-10/IL-10R1/IL-10R2 and IL-22/IL-22R1/IL-10R2 ternary complexes. The models reveal a conserved binding epitope that is surrounded by two clefts that accommodate the structural and chemical diversity of the cytokines. These results provide a structural framework for interpreting IL-10R2 single nucleotide polymorphisms associated with human disease. PubMed: 20462497DOI: 10.1016/j.str.2010.02.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
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