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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDEZ8 |
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![]() | Interleukin-18 receptor accessory protein, IL-18Rβ-ECD
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Function / homology | ![]() 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 |
Biological species | ![]() |
![]() | ![]() 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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #2663 | ![]() Type: atomic / Chi-square value: 2.32931416757 ![]() |
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Model #2664 | ![]() Type: atomic / Chi-square value: 2.32931416757 ![]() |
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Sample
![]() | Name: Interleukin-18 receptor accessory protein, IL-18Rβ-ECD Specimen concentration: 10 mg/ml |
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Buffer | Name: 10mM HEPES, 150mM NaCl, 3% glycerol / pH: 7.2 |
Entity #1396 | Type: 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 |
-Experimental information
Beam | Instrument name: Advanced Light Source (ALS) 12.3.1 (SIBYLS) City: Berkeley, CA / 国: USA ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus3 X 2M / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Jul 24, 2017 / Cell temperature: 20 °C / Exposure time: 3 sec. / Number of frames: 600 / Unit: 1/A /
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Distance distribution function P(R) |
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Result | 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.
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