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1n6u
From Proteopedia
(New page: 200px<br /> <applet load="1n6u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n6u" /> '''NMR structure of the interferon-binding ect...) |
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| - | [[Image:1n6u.gif|left|200px]]<br /> | + | [[Image:1n6u.gif|left|200px]]<br /><applet load="1n6u" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1n6u" size=" | + | |
caption="1n6u" /> | caption="1n6u" /> | ||
'''NMR structure of the interferon-binding ectodomain of the human interferon receptor'''<br /> | '''NMR structure of the interferon-binding ectodomain of the human interferon receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The potent antiviral and antiproliferative activities of human type I | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N6U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1N6U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Anglister, J.]] | [[Category: Anglister, J.]] | ||
| - | [[Category: Chill, J | + | [[Category: Chill, J H.]] |
[[Category: Levy, R.]] | [[Category: Levy, R.]] | ||
| - | [[Category: Quadt, S | + | [[Category: Quadt, S R.]] |
[[Category: Schreiber, G.]] | [[Category: Schreiber, G.]] | ||
[[Category: fibronectin fold]] | [[Category: fibronectin fold]] | ||
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[[Category: two-domain structure]] | [[Category: two-domain structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:52 2008'' |
Revision as of 12:02, 21 February 2008
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NMR structure of the interferon-binding ectodomain of the human interferon receptor
Contents |
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
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 Thu Feb 21 14:02:52 2008
