3S8W
D2 domain of human IFNAR2
Summary for 3S8W
| Entry DOI | 10.2210/pdb3s8w/pdb |
| Related | 3S98 3S9D |
| Descriptor | Interferon alpha/beta receptor 2, CHLORIDE ION (3 entities in total) |
| Functional Keywords | human, type i interferons, receptor chain, ifnar2, fibronectin type iii module, part of type i interferon receptor chain, interferon, extracellular space, signaling protein receptor |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Membrane; Single-pass type I membrane protein. Isoform 2: Membrane; Single-pass type I membrane protein. Isoform 3: Secreted: P48551 |
| Total number of polymer chains | 3 |
| Total formula weight | 36212.73 |
| Authors | Thomas, C.,Garcia, K.C. (deposition date: 2011-05-31, release date: 2011-08-31, Last modification date: 2024-11-27) |
| Primary citation | Thomas, C.,Moraga, I.,Levin, D.,Krutzik, P.O.,Podoplelova, Y.,Trejo, A.,Lee, C.,Yarden, G.,Vleck, S.E.,Glenn, J.S.,Nolan, G.P.,Piehler, J.,Schreiber, G.,Garcia, K.C. Structural linkage between ligand discrimination and receptor activation by type I interferons. Cell(Cambridge,Mass.), 146:621-632, 2011 Cited by PubMed Abstract: Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer. Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects. The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs. Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity. Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns. PubMed: 21854986DOI: 10.1016/j.cell.2011.06.048 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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