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- SASDE79: Interleukin-18 receptor 1, IL-18Rα-ECD (Interleukin-18 receptor 1) -

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Basic information

Entry
Database: SASBDB / ID: SASDE79
SampleInterleukin-18 receptor 1, IL-18Rα-ECD
  • Interleukin-18 receptor 1 (protein), Homo sapiens
Function / homology
Function and homology information


interleukin-18 binding / interleukin-18 receptor activity / interleukin-18 receptor complex / interleukin-1 receptor activity / T-helper 1 cell differentiation / Interleukin-18 signaling / positive regulation of T-helper 1 cell cytokine production / interleukin-18-mediated signaling pathway / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity, cyclic ADP-ribose generating ...interleukin-18 binding / interleukin-18 receptor activity / interleukin-18 receptor complex / interleukin-1 receptor activity / T-helper 1 cell differentiation / Interleukin-18 signaling / positive regulation of T-helper 1 cell cytokine production / interleukin-18-mediated signaling pathway / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity, cyclic ADP-ribose generating / Interleukin-37 signaling / natural killer cell activation / negative regulation of cold-induced thermogenesis / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of type II interferon production / positive regulation of NF-kappaB transcription factor activity / signaling receptor activity / adaptive immune response / immune response / inflammatory response / cell surface / signal transduction / plasma membrane
Similarity search - Function
Interleukin-1 receptor type I/II / Interleukin-1 receptor family / TIR domain / Toll - interleukin 1 - resistance / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. ...Interleukin-1 receptor type I/II / Interleukin-1 receptor family / TIR domain / Toll - interleukin 1 - resistance / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Interleukin-18 receptor 1
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationJournal: Structure / Year: 2019
Title: Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling.
Authors: Jiwan Ge / Soumya G Remesh / Michal Hammel / Si Pan / Andrew D Mahan / Shuying Wang / Xinquan Wang /
Abstract: The interleukin 1 (IL-1) receptor family, whose members contain three immunoglobulin-like domains (D1-D3) in the extracellular region, is responsible for transmitting pleiotropic signals of IL-1 ...The interleukin 1 (IL-1) receptor family, whose members contain three immunoglobulin-like domains (D1-D3) in the extracellular region, is responsible for transmitting pleiotropic signals of IL-1 cytokines. The inter-domain flexibility of IL-1 receptors and its functional roles have not been fully elucidated. In this study, we used small-angle X-ray scattering to show that ligand-binding primary receptors and co-receptors in the family all have inherent inter-domain flexibility due to the D2/D3 linker. Variants of the IL-1RAcP and IL-18Rβ co-receptors with mutated D2/D3 linkers cannot form a cytokine-receptor complex and mediate signaling. Our analysis further revealed that these mutated co-receptors exhibited a changed conformational ensemble, suggesting that loss of function is due to the alteration of receptor dynamics. Taken together, our results demonstrate that the D2/D3 linker is a critical functional determinant of IL-1 receptor and underscore the important roles of the inter-domain flexibility in cytokine/receptor binding and signaling.
Contact author
  • Shu-Ying Wang (National Cheng Kung University, Taiwan)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #2685
Type: atomic / Chi-square value: 1.41925617646
Search similar-shape structures of this assembly by Omokage search (details)
Model #2686
Type: atomic / Chi-square value: 1.41925617646
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Interleukin-18 receptor 1, IL-18Rα-ECD / Specimen concentration: 10 mg/ml
BufferName: 10mM HEPES, 150mM NaCl, 3% glycerol / pH: 7.2
Entity #1395Type: protein / Description: Interleukin-18 receptor 1 / Formula weight: 36.302 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q13478
Sequence: CTSRPHITVV EGEPFYLKHC SCSLAHEIET TTKSWYKSSG SQEHVELNPR SSSRIALHDC VLEFWPVELN DTGSYFFQMK NYTQKWKLNV IRRNKHSCFT ERQVTSKIVE VKKFFQITCE NSYYQTLVNS TSLYKNCKKL LLENNKNPTI KKNAEFEDQG YYSCVHFLHH ...Sequence:
CTSRPHITVV EGEPFYLKHC SCSLAHEIET TTKSWYKSSG SQEHVELNPR SSSRIALHDC VLEFWPVELN DTGSYFFQMK NYTQKWKLNV IRRNKHSCFT ERQVTSKIVE VKKFFQITCE NSYYQTLVNS TSLYKNCKKL LLENNKNPTI KKNAEFEDQG YYSCVHFLHH NGKLFNITKT FNITIVEDRS NIVPVLLGPK LNHVAVELGK NVRLNCSALL NEEDVIYWMF GEENGSDPNI HEEKEMRIMT PEGKWHASKV LRIENIGESN LNVLYNCTVA STGGTDTKSF ILVRKADMAD IPGHVFTRHH HHHH

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Experimental information

BeamInstrument name: Advanced Light Source (ALS) 12.3.1 (SIBYLS)
City: Berkeley, CA / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.103 Å / Dist. spec. to detc.: 1.5 mm
DetectorName: MAR 165 CCD
Scan
Title: Interleukin-18 receptor 1, IL-18Rα-ECD / Measurement date: Oct 3, 2014 / Cell temperature: 20 °C / Exposure time: 3 sec. / Number of frames: 600 / Unit: 1/A /
MinMax
Q0.0131 0.3299
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 385 /
MinMax
Q0.01855 0.2521
P(R) point10 394
R0 108.6
Result
Type of curve: sec
Comments: SEC-SAXS was performed at 20°C using the following parameters: Column: Schodex kw-803 ; Flow rate: 0.5 mL/min; Total acquisition time: 30min; Sample injection concentration: 10 mg/mL; Injection volume: 50 μL.
ExperimentalPorod
MW55.1 kDa-
Volume-77 nm3

P(R)GuinierGuinier error
Forward scattering, I0221.5 218.9 0.6
Radius of gyration, Rg3.27 nm3.147 nm0.01

MinMax
D-10.86
Guinier point1 48

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