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1n6u
From Proteopedia
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[[Image:1n6u.gif|left|200px]] | [[Image:1n6u.gif|left|200px]] | ||
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'''NMR structure of the interferon-binding ectodomain of the human interferon receptor''' | '''NMR structure of the interferon-binding ectodomain of the human interferon receptor''' | ||
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[[Category: Quadt, S R.]] | [[Category: Quadt, S R.]] | ||
[[Category: Schreiber, G.]] | [[Category: Schreiber, G.]] | ||
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| - | [[Category: | + | [[Category: Immunoglobulin fold]] |
| - | [[Category: | + | [[Category: Two-domain structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:10:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:10, 2 May 2008
NMR structure of the interferon-binding ectodomain of the human interferon receptor
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.
About this Structure
1N6U 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 Sat May 3 02:10:08 2008
