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- PDB-9ot1: Helical assembly of the IL-17RA/RB/ACT1 complex -

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Basic information

Entry
Database: PDB / ID: 9ot1
TitleHelical assembly of the IL-17RA/RB/ACT1 complex
Components
  • E3 ubiquitin ligase TRAF3IP2
  • Interleukin-17 receptor B,Interleukin-17 receptor A
KeywordsSIGNALING PROTEIN / IL-17 receptor / ACT1 / helical assembly / IL-17
Function / homology
Function and homology information


transitional two stage B cell differentiation / eosinophil mediated immunity / protein localization to P-body / interleukin-17 receptor activity / leukocyte activation involved in inflammatory response / granulocyte chemotaxis / Interleukin-17 signaling / establishment of T cell polarity / T-helper 17 type immune response / interleukin-17A-mediated signaling pathway ...transitional two stage B cell differentiation / eosinophil mediated immunity / protein localization to P-body / interleukin-17 receptor activity / leukocyte activation involved in inflammatory response / granulocyte chemotaxis / Interleukin-17 signaling / establishment of T cell polarity / T-helper 17 type immune response / interleukin-17A-mediated signaling pathway / positive regulation of interleukin-23 production / positive regulation of chemokine (C-X-C motif) ligand 1 production / CD40 signaling pathway / mucus secretion / interleukin-17-mediated signaling pathway / eosinophil homeostasis / B cell affinity maturation / positive regulation of interleukin-13 production / positive regulation of interleukin-5 production / fibroblast activation / neutrophil activation / B cell apoptotic process / mRNA stabilization / positive regulation of cytokine production involved in inflammatory response / cytokine receptor activity / type 2 immune response / signal transduction involved in regulation of gene expression / extrinsic component of cytoplasmic side of plasma membrane / skin development / B cell homeostasis / humoral immune response / T cell differentiation / protein K63-linked ubiquitination / lymph node development / defense response to fungus / spleen development / positive regulation of defense response to virus by host / tumor necrosis factor-mediated signaling pathway / regulation of cell growth / kidney development / protein catabolic process / defense response / RING-type E3 ubiquitin transferase / positive regulation of interleukin-6 production / response to virus / protein import into nucleus / positive regulation of inflammatory response / ubiquitin protein ligase activity / heart development / cytoplasmic vesicle / cell surface receptor signaling pathway / positive regulation of canonical NF-kappaB signal transduction / intracellular signal transduction / response to xenobiotic stimulus / inflammatory response / signaling receptor binding / innate immune response / intracellular membrane-bounded organelle / SARS-CoV-2 activates/modulates innate and adaptive immune responses / cell surface / extracellular region / nucleus / membrane / plasma membrane / cytoplasm
Similarity search - Function
: / Interleukin-17 receptor, fibronectin-III-like domain 1 / Interleukin-17 receptor A/B, FnIII-like domain 1 superfamily / Interleukin-17 receptor A/B, FnIII-like domain 2 superfamily / Interleukin-17 receptor, fibronectin-III-like domain 1 / Interleukin 17 receptor D / Interleukin-17 receptor-like / SEFIR domain / SEFIR domain / SEFIR domain profile.
Similarity search - Domain/homology
E3 ubiquitin ligase TRAF3IP2 / Interleukin-17 receptor A / Interleukin-17 receptor B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å
AuthorsZhang, H. / Bai, X. / Zhang, X.
Funding support United States, 4items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM130289 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM156386 United States
Welch FoundationI-1702 United States
Welch FoundationI-1944 United States
CitationJournal: Nat Commun / Year: 2025
Title: Structural basis for ACT1 oligomerization induced by IL-17 receptor hetero-tetramer.
Authors: Hui Zhang / Xiao-Chen Bai / Xuewu Zhang /
Abstract: The IL-17 receptors (IL-17Rs) play critical roles in immunity and inflammatory diseases. IL-17-induced heteromeric complexes between IL-17RA and another IL-17R trigger signaling by binding the ...The IL-17 receptors (IL-17Rs) play critical roles in immunity and inflammatory diseases. IL-17-induced heteromeric complexes between IL-17RA and another IL-17R trigger signaling by binding the downstream transducer ACT1 through interactions between their intracellular SEF/IL-17R (SEFIR) domains. The molecular mechanism of this process remains unclear. Here we present the cryo-EM structure of the complex of IL-17RA, IL-17RB and ACT1, showing that the IL-17RA and IL-17RB SEFIR domains form an asymmetric hetero-tetramer. The two IL-17RA SEFIR domains serve as the base to recruit ACT1, while IL-17RB stabilizes the IL-17RA dimer but makes no interaction with ACT1. IL-17RB, IL-17RA, and multiple ACT1 together form a double-stranded helical assembly. The C-terminal SEFIR extension (SEFEX) of IL-17RA acts as a molecular tendril to help anchor the ACT1 protomers. The structural model is supported by our mutational analyses. These findings reveal the basis for the formation for the signalosome of the IL-17 receptors and ACT1 critical for immune signaling.
History
DepositionMay 26, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 17, 2025Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: Interleukin-17 receptor B,Interleukin-17 receptor A
A: Interleukin-17 receptor B,Interleukin-17 receptor A
C: Interleukin-17 receptor B,Interleukin-17 receptor A
D: Interleukin-17 receptor B,Interleukin-17 receptor A
E: E3 ubiquitin ligase TRAF3IP2
F: E3 ubiquitin ligase TRAF3IP2
G: E3 ubiquitin ligase TRAF3IP2
H: E3 ubiquitin ligase TRAF3IP2
I: E3 ubiquitin ligase TRAF3IP2
J: E3 ubiquitin ligase TRAF3IP2
K: E3 ubiquitin ligase TRAF3IP2
L: E3 ubiquitin ligase TRAF3IP2
M: E3 ubiquitin ligase TRAF3IP2
N: E3 ubiquitin ligase TRAF3IP2
O: E3 ubiquitin ligase TRAF3IP2
P: E3 ubiquitin ligase TRAF3IP2
Q: E3 ubiquitin ligase TRAF3IP2
R: E3 ubiquitin ligase TRAF3IP2
S: E3 ubiquitin ligase TRAF3IP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)658,36621
Polymers658,23519
Non-polymers1312
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Interleukin-17 receptor B,Interleukin-17 receptor A / IL-17 receptor B / IL-17RB / Cytokine receptor-like 4 / IL-17 receptor homolog 1 / IL-17Rh1 / ...IL-17 receptor B / IL-17RB / Cytokine receptor-like 4 / IL-17 receptor homolog 1 / IL-17Rh1 / IL17Rh1 / Interleukin-17B receptor / IL-17B receptor / IL-17 receptor A / IL-17RA / CDw217


Mass: 74795.617 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: IL17RB, CRL4, EVI27, IL17BR, UNQ2501/PRO19612, IL17RA, IL17R
Production host: Homo sapiens (human) / References: UniProt: Q9NRM6, UniProt: Q96F46
#2: Protein
E3 ubiquitin ligase TRAF3IP2 / Adapter protein CIKS / Connection to IKK and SAPK/JNK / E3 ubiquitin-protein ligase CIKS / Nuclear ...Adapter protein CIKS / Connection to IKK and SAPK/JNK / E3 ubiquitin-protein ligase CIKS / Nuclear factor NF-kappa-B activator 1 / ACT1 / TRAF3-interacting protein 2


Mass: 23936.861 Da / Num. of mol.: 15
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRAF3IP2, C6orf2, C6orf4, C6orf5, C6orf6 / Production host: Homo sapiens (human)
References: UniProt: O43734, RING-type E3 ubiquitin transferase
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
Has ligand of interestN
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: helical assembly of the IL-17RA/RB/ACT1 complex / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Molecular weightValue: 0.51 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: NITROGEN

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.21.1_5286 / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 157029 / Symmetry type: POINT
RefinementHighest resolution: 3 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00429420
ELECTRON MICROSCOPYf_angle_d0.45739844
ELECTRON MICROSCOPYf_dihedral_angle_d9.95411190
ELECTRON MICROSCOPYf_chiral_restr0.0414413
ELECTRON MICROSCOPYf_plane_restr0.0045079

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