1n6v
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1n6v.gif|left|200px]] | [[Image:1n6v.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1n6v", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1n6v| PDB=1n6v | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''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''' | ||
| Line 30: | Line 27: | ||
[[Category: Quadt, S R.]] | [[Category: Quadt, S R.]] | ||
[[Category: Schreiber, G.]] | [[Category: Schreiber, G.]] | ||
| - | [[Category: | + | [[Category: Fibronectin fold]] |
| - | [[Category: | + | [[Category: Immunoglobulin fold]] |
| - | [[Category: | + | [[Category: Two-domain structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:10:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:10, 2 May 2008
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
