1n6v | pdb_00001n6v
Average structure of the interferon-binding ectodomain of the human type I interferon receptor
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Overview
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.
Disease
Known disease associated with this structure: Hepatitis B virus, susceptibility to OMIM:[602376]
About this Structure
1N6V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding., Chill JH, Quadt SR, Levy R, Schreiber G, Anglister J, Structure. 2003 Jul;11(7):791-802. PMID:12842042
Page seeded by OCA on Mon Nov 12 18:18:32 2007
