1N6V

Average structure of the interferon-binding ectodomain of the human type I interferon receptor

1N6V の概要

• エントリーDOI: 10.2210/pdb1n6v/pdb
• 関連するPDBエントリー: 1N6U
• NMR情報: BMRB: 5049
• 分子名称: Interferon-alpha/beta receptor beta chain (1 entity in total)
• 機能のキーワード: immunoglobulin fold, fibronectin fold, two-domain structure, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Membrane; Single-pass type I membrane protein. Isoform 2: Membrane; Single-pass type I membrane protein. Isoform 3: Secreted: P48551
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24323.44

構造登録者

Chill, J.H.,Quadt, S.R.,Levy, R.,Schreiber, G.,Anglister, J. (登録日: 2002-11-12, 公開日: 2003-07-15, 最終更新日: 2024-10-30)

主引用文献

Chill, J.H.,Quadt, S.R.,Levy, R.,Schreiber, G.,Anglister, J.
The human type I interferon receptor. NMR structure reveals the molecular basis of ligand binding.
Structure, 11:791-802, 2003

PubMed Abstract: The potent antiviral and antiproliferative activities of human type I interferons (IFNs) are mediated by a single receptor comprising two subunits, IFNAR1 and IFNAR2. The structure of the IFNAR2 IFN binding ectodomain (IFNAR2-EC), the first helical cytokine receptor structure determined in solution, reveals the molecular basis for IFN binding. The atypical perpendicular orientation of its two fibronectin domains explains the lack of C domain involvement in ligand binding. A model of the IFNAR2-EC/IFNalpha2 complex based on double mutant cycle-derived constraints uncovers an extensive and predominantly aliphatic hydrophobic patch on the receptor that interacts with a matching hydrophobic surface of IFNalpha2. An adjacent motif of alternating charged side chains guides the two proteins into a tight complex. The binding interface may account for crossreactivity and ligand specificity of the receptor. This molecular description of IFN binding should be invaluable for study and design of IFN-based biomedical agents.

PubMed: 12842042
DOI: 10.1016/S0969-2126(03)00120-5

実験手法

SOLUTION NMR