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- SASDE89: Interleukin-1 receptor accessory protein ectodomain with RII linker -

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Basic information

Entry
Database: SASBDB / ID: SASDE89
SampleInterleukin-1 receptor accessory protein ectodomain with RII linker
  • Interleukin-1 receptor accessory protein ectodomains with RII linker (protein), Homo sapiens
Function / homology
Function and homology information


Interleukin-33 signaling / interleukin-33 receptor activity / Interleukin-36 pathway / interleukin-1 receptor activity / trans-synaptic signaling by trans-synaptic complex / Receptor-type tyrosine-protein phosphatases / regulation of postsynaptic density assembly / synaptic membrane adhesion / interleukin-33-mediated signaling pathway / positive regulation of interleukin-13 production ...Interleukin-33 signaling / interleukin-33 receptor activity / Interleukin-36 pathway / interleukin-1 receptor activity / trans-synaptic signaling by trans-synaptic complex / Receptor-type tyrosine-protein phosphatases / regulation of postsynaptic density assembly / synaptic membrane adhesion / interleukin-33-mediated signaling pathway / positive regulation of interleukin-13 production / positive regulation of interleukin-5 production / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity / NAD+ nucleotidase, cyclic ADP-ribose generating / interleukin-1 receptor binding / positive regulation of synapse assembly / interleukin-1-mediated signaling pathway / positive regulation of interleukin-4 production / regulation of presynapse assembly / coreceptor activity / positive regulation of interleukin-6 production / Interleukin-1 signaling / PIP3 activates AKT signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protein-containing complex assembly / inflammatory response / immune response / innate immune response / glutamatergic synapse / extracellular region / membrane / plasma membrane
Similarity search - Function
Interleukin-1 receptor type I/II / 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 ...Interleukin-1 receptor type I/II / 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-1 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

Downloads & links

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Models

Model #2687
Type: atomic / Chi-square value: 1.55136035699
Search similar-shape structures of this assembly by Omokage search (details)
Model #2688
Type: atomic / Chi-square value: 1.55136035699
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Interleukin-1 receptor accessory protein ectodomain with RII linker
Specimen concentration: 7.8 mg/ml
BufferName: 10mM HEPES, 150mM NaCl, 3% glycerol / pH: 7.2
Entity #1397Type: protein
Description: Interleukin-1 receptor accessory protein ectodomains with RII linker
Formula weight: 40.893 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q9NPH3
Sequence: SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKFNYST AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY IEYGIQRITC PNVDGYFPSS VKPTITWYMG CYKIQNFNNV ...Sequence:
SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKFNYST AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY IEYGIQRITC PNVDGYFPSS VKPTITWYMG CYKIQNFNNV IPEGMNLSFL IALISNNGNY TCVVTYPENG RTFHLTRTLT VKVKKKKEET IPVIHSPNDH VVYEKEPGEE LLIPCTVYFS FLMDSRNEVW WTIDGKKPDD ITIDVTINES ISHSRTEDET RTQILSIKKV TSEDLKRSYV CHARSAKGEV AKAAKVKAAA LHHILDAQKM VWNHRHHHHH H

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Experimental information

BeamInstrument name: Advanced Light Source (ALS) 12.3.1 (SIBYLS)
City: Berkeley, CA / : 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-1 receptor accessory protein ectodomain with RII linker
Measurement date: Jul 24, 2017 / Cell temperature: 20 °C / Exposure time: 3 sec. / Number of frames: 600 / Unit: 1/A /
MinMax
Q0.0131 0.5608
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 430 /
MinMax
Q0.02313 0.2623
P(R) point19 448
R0 106.6
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: 7.8 mg/mL; ...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: 7.8 mg/mL; Injection volume: 50 μL.
ExperimentalPorod
MW50.2 kDa-
Volume-75 nm3

P(R)GuinierGuinier error
Forward scattering, I0345.1 342.7 0.9
Radius of gyration, Rg3.12 nm3.043 nm0.1

MinMax
D-10.66
Guinier point7 54

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