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1n6v

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Revision as of 18:54, 20 November 2019

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

Structural highlights

1n6v is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1n6u
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[INAR2_HUMAN] Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Novick D, Cohen B, Rubinstein M. The human interferon alpha/beta receptor: characterization and molecular cloning. Cell. 1994 May 6;77(3):391-400. PMID:8181059
↑ Domanski P, Witte M, Kellum M, Rubinstein M, Hackett R, Pitha P, Colamonici OR. Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling. J Biol Chem. 1995 Sep 15;270(37):21606-11. PMID:7665574
↑ Novick D, Cohen B, Tal N, Rubinstein M. Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor. J Leukoc Biol. 1995 May;57(5):712-8. PMID:7759950
↑ Wagner TC, Velichko S, Vogel D, Rani MR, Leung S, Ransohoff RM, Stark GR, Perez HD, Croze E. Interferon signaling is dependent on specific tyrosines located within the intracellular domain of IFNAR2c. Expression of IFNAR2c tyrosine mutants in U5A cells. J Biol Chem. 2002 Jan 11;277(2):1493-9. Epub 2001 Oct 26. PMID:11682488 doi:10.1074/jbc.M108928200
↑ Velichko S, Wagner TC, Turkson J, Jove R, Croze E. STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c. Activation of multiple STATS proceeds through the redundant usage of two tyrosine residues. J Biol Chem. 2002 Sep 20;277(38):35635-41. Epub 2002 Jun 24. PMID:12105218 doi:10.1074/jbc.M204578200
↑ Chill JH, Quadt SR, Levy R, Schreiber G, Anglister J. The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding. Structure. 2003 Jul;11(7):791-802. PMID:12842042

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n6v"

@@ Line 1: / Line 1: @@
 ==Average structure of the interferon-binding ectodomain of the human type I interferon receptor==
-<StructureSection load='1n6v' size='340' side='right' caption='[[1n6v]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1n6v' size='340' side='right'caption='[[1n6v]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1n6v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N6V FirstGlance]. <br>
@@ Line 28: / Line 28: @@
 </div>
 <div class="pdbe-citations 1n6v" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Interferon receptor 3D structures|Interferon receptor 3D structures]]
+*[[Multiple sclerosis|Multiple sclerosis]]
 == References ==
 <references/>
@@ Line 33: / Line 37: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Anglister, J]]
 [[Category: Chill, J H]]

1n6v

From Proteopedia

Revision as of 18:54, 20 November 2019

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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