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- SASDEZ8: Interleukin-18 receptor accessory protein, IL-18Rβ-ECD -

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Basic information

Entry
Database: SASBDB / ID: SASDEZ8
SampleInterleukin-18 receptor accessory protein, IL-18Rβ-ECD
  • Interleukin-18 receptor accessory protein (protein), Homo sapiens
Function / homology
Function and homology information


interleukin-18 receptor activity / interleukin-18 receptor complex / Interleukin-18 signaling / positive regulation of natural killer cell mediated cytotoxicity / neutrophil activation / interleukin-18-mediated signaling pathway / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity / NAD+ nucleotidase, cyclic ADP-ribose generating / coreceptor activity ...interleukin-18 receptor activity / interleukin-18 receptor complex / Interleukin-18 signaling / positive regulation of natural killer cell mediated cytotoxicity / neutrophil activation / interleukin-18-mediated signaling pathway / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity / NAD+ nucleotidase, cyclic ADP-ribose generating / coreceptor activity / cellular response to hydrogen peroxide / positive regulation of NF-kappaB transcription factor activity / cell population proliferation / inflammatory response / immune response / plasma membrane
Similarity search - Function
IL-1Ra-like, immunoglobulin domain / Immunoglobulin domain / 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 ...IL-1Ra-like, immunoglobulin domain / Immunoglobulin domain / 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 accessory protein
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 #2663
Type: atomic / Chi-square value: 2.32931416757
Search similar-shape structures of this assembly by Omokage search (details)
Model #2664
Type: atomic / Chi-square value: 2.32931416757
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Interleukin-18 receptor accessory protein, IL-18Rβ-ECD
Specimen concentration: 10 mg/ml
BufferName: 10mM HEPES, 150mM NaCl, 3% glycerol / pH: 7.2
Entity #1396Type: protein / Description: Interleukin-18 receptor accessory protein / Formula weight: 41.363 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: O95256
Sequence: FNISGCSTKK LLWTYSTRSE EEFVLFCDLP EPQKSHFCHR NRLSPKQVPE HLPFMGSNDL SDVQWYQQPS NGDPLEDIRK SYPHIIQDKC TLHFLTPGVN NSGSYICRPK MIKSPYDVAC CVKMILEVKP QTNASCEYSA SHKQDLLLGS TGSISCPSLS CQSDAQSPAV ...Sequence:
FNISGCSTKK LLWTYSTRSE EEFVLFCDLP EPQKSHFCHR NRLSPKQVPE HLPFMGSNDL SDVQWYQQPS NGDPLEDIRK SYPHIIQDKC TLHFLTPGVN NSGSYICRPK MIKSPYDVAC CVKMILEVKP QTNASCEYSA SHKQDLLLGS TGSISCPSLS CQSDAQSPAV TWYKNGKLLS VERSNRIVVD EVYDYHQGTY VCDYTQSDTV SSWTVRAVVQ VRTIVGDTKL KPDILDPVED TLEVELGKPL TISCKARFGF ERVFNPVIKW YIKDSDLEWE VSVPEAKSIK STLKDEIIER NIILEKVTQR DLRRKFVCFV QNSIGNTTQS VQLKEKRAAA LHHILDAQKM VWNHRHHHHH H

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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: Pilatus3 X 2M / Pixsize x: 172 mm
Scan
Title: Interleukin-18 receptor accessory protein IL-18Rβ-ECD
Measurement date: Jul 24, 2017 / Cell temperature: 20 °C / Exposure time: 3 sec. / Number of frames: 600 / Unit: 1/A /
MinMax
Q0.012 0.5664
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 402 /
MinMax
Q0.02035 0.2439
P(R) point16 417
R0 114.6
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
MW55.9 kDa-
Volume-70 nm3

P(R)GuinierGuinier error
Forward scattering, I0255 257.05 0.82
Radius of gyration, Rg3.33 nm3.274 nm0.01

MinMax
D-11.46
Guinier point1 51

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