1n6v

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[[Image:1n6v.gif|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1n6u|1N6U]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6v OCA], [http://www.ebi.ac.uk/pdbsum/1n6v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n6v RCSB]</span>
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'''Average structure of the interferon-binding ectodomain of the human type I interferon receptor'''
'''Average structure of the interferon-binding ectodomain of the human type I 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: fibronectin fold]]
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[[Category: Fibronectin fold]]
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[[Category: immunoglobulin fold]]
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[[Category: Immunoglobulin fold]]
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[[Category: two-domain structure]]
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[[Category: Two-domain structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:10:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:26:12 2008''
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Revision as of 23:10, 2 May 2008

Template:STRUCTURE 1n6v

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

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 Sat May 3 02:10:17 2008

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