3S98

human IFNAR1

3S98 の概要

• エントリーDOI: 10.2210/pdb3s98/pdb
• 関連するPDBエントリー: 3S8W 3S9D
• 分子名称: Interferon alpha/beta receptor 1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: human, type i interferons, receptor chain, ifnar1, fibronectin type iii, type i interferon receptor chain, extracellular space, signaling protein receptor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35863.02

構造登録者

Thomas, C.,Garcia, K.C. (登録日: 2011-06-01, 公開日: 2011-08-31, 最終更新日: 2024-11-20)

主引用文献

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

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: 21854986
DOI: 10.1016/j.cell.2011.06.048

実験手法

X-RAY DIFFRACTION (1.9 Å)