1n6v
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1n6v.gif|left|200px]] | + | [[Image:1n6v.gif|left|200px]] |
- | + | ||
- | '''Average structure of the interferon-binding ectodomain of the human type I interferon receptor''' | + | {{Structure |
+ | |PDB= 1n6v |SIZE=350|CAPTION= <scene name='initialview01'>1n6v</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Average structure of the interferon-binding ectodomain of the human type I interferon receptor''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
- | 1N6V is a [ | + | 1N6V is a [[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=1N6V OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12842042 12842042] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 25: | Line 34: | ||
[[Category: two-domain structure]] | [[Category: two-domain structure]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:59 2008'' |
Revision as of 10:52, 20 March 2008
| |||||||
Coordinates: | save as pdb, mmCIF, xml |
Average structure of the interferon-binding ectodomain of the human type I 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
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 Thu Mar 20 12:52:59 2008