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Yorodumi- PDB-1n6u: NMR structure of the interferon-binding ectodomain of the human i... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1n6u | ||||||
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Title | NMR structure of the interferon-binding ectodomain of the human interferon receptor | ||||||
Components | Interferon-alpha/beta receptor beta chain | ||||||
Keywords | IMMUNE SYSTEM / immunoglobulin fold / fibronectin fold / two-domain structure | ||||||
Function / homology | Function and homology information type I interferon receptor activity / type I interferon binding / interleukin-22 receptor activity / JAK pathway signal transduction adaptor activity / response to interferon-beta / response to interferon-alpha / type I interferon-mediated signaling pathway / cytokine binding / cell surface receptor signaling pathway via JAK-STAT / Regulation of IFNA/IFNB signaling ...type I interferon receptor activity / type I interferon binding / interleukin-22 receptor activity / JAK pathway signal transduction adaptor activity / response to interferon-beta / response to interferon-alpha / type I interferon-mediated signaling pathway / cytokine binding / cell surface receptor signaling pathway via JAK-STAT / Regulation of IFNA/IFNB signaling / cellular response to interferon-beta / response to virus / Evasion by RSV of host interferon responses / cellular response to virus / Interferon alpha/beta signaling / Potential therapeutics for SARS / defense response to virus / cell surface receptor signaling pathway / protein kinase binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Chill, J.H. / Quadt, S.R. / Levy, R. / Schreiber, G. / Anglister, J. | ||||||
Citation | Journal: Structure / Year: 2003 Title: The human type I interferon receptor. NMR structure reveals the molecular basis of ligand binding. Authors: Chill, J.H. / Quadt, S.R. / Levy, R. / Schreiber, G. / Anglister, J. #1: Journal: Biochemistry / Year: 2002 Title: The human interferon receptor: NMR-based modeling, mapping of the IFN-alpha2 binding site, and observed ligand-induced tightening Authors: Chill, J.H. / Nivasch, R. / Levy, R. / Albeck, S. / Schreiber, G. / Anglister, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n6u.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1n6u.ent.gz | 1.2 MB | Display | PDB format |
PDBx/mmJSON format | 1n6u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n6/1n6u ftp://data.pdbj.org/pub/pdb/validation_reports/n6/1n6u | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 24323.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IFNAR2 OR IFNARB / Production host: Escherichia coli (E. coli) / Strain (production host): TG1 / References: UniProt: P48551 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: Experiments all performed in Shigemi tubed equipped with inserts |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 1947 inter-residual NOE-derived distance restraints (of which 1066 are long range), 172 dihedral angle restraints (88 experimental and 84 TALOS-derived) ...Details: the structures are based on a total of 1947 inter-residual NOE-derived distance restraints (of which 1066 are long range), 172 dihedral angle restraints (88 experimental and 84 TALOS-derived), 138 distance restraints from hydrogen bonds, and 109 residual dipolar coupling restraints. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 35 / Conformers submitted total number: 22 |