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- EMDB-70818: Helical assembly of the IL-17RA/RB/ACT1 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-70818
TitleHelical assembly of the IL-17RA/RB/ACT1 complex
Map data
Sample
  • Complex: helical assembly of the IL-17RA/RB/ACT1 complex
    • Protein or peptide: Interleukin-17 receptor B,Interleukin-17 receptor A
    • Protein or peptide: E3 ubiquitin ligase TRAF3IP2
  • Ligand: ZINC ION
KeywordsIL-17 receptor / ACT1 / helical assembly / IL-17 / SIGNALING PROTEIN
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)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsZhang H / Bai X / Zhang X
Funding support United States, 4 items
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, 2025-
Header (metadata) releaseDec 17, 2025-
Map releaseDec 17, 2025-
UpdateDec 31, 2025-
Current statusDec 31, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_70818.png

Downloads & links

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Map

FileDownload / File: emd_70818.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 400 pix.
= 428. Å		1.07 Å/pix.
x 400 pix.
= 428. Å		1.07 Å/pix.
x 400 pix.
= 428. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 5.0
Minimum - Maximum-12.77256 - 33.333157
Average (Standard dev.)0.03599623 (±0.58216643)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 428.00003 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_70818_msk_1.map
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Half map: #2

Fileemd_70818_half_map_1.map
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Half map: #1

Fileemd_70818_half_map_2.map
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Sample components

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Entire : helical assembly of the IL-17RA/RB/ACT1 complex

EntireName: helical assembly of the IL-17RA/RB/ACT1 complex
Components
  • Complex: helical assembly of the IL-17RA/RB/ACT1 complex
    • Protein or peptide: Interleukin-17 receptor B,Interleukin-17 receptor A
    • Protein or peptide: E3 ubiquitin ligase TRAF3IP2
  • Ligand: ZINC ION

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Supramolecule #1: helical assembly of the IL-17RA/RB/ACT1 complex

SupramoleculeName: helical assembly of the IL-17RA/RB/ACT1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 510 KDa

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Macromolecule #1: Interleukin-17 receptor B,Interleukin-17 receptor A

MacromoleculeName: Interleukin-17 receptor B,Interleukin-17 receptor A / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 74.795617 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GPLELLPPIK VLVVYPSEIC FHHTICYFTE FLQNHCRSEV ILEKWQKKKI AEMGPVQWLA TQKKAADKVV FLLSNDVNSV CDGTCGKSE GSPSENSQDL FPLAFNLFCS DLRSQIHLHK YVVVYFREID TKDDYNALSV CPKYHLMKDA TAFCAELLHV K QGGGSGGG ...String:
GPLELLPPIK VLVVYPSEIC FHHTICYFTE FLQNHCRSEV ILEKWQKKKI AEMGPVQWLA TQKKAADKVV FLLSNDVNSV CDGTCGKSE GSPSENSQDL FPLAFNLFCS DLRSQIHLHK YVVVYFREID TKDDYNALSV CPKYHLMKDA TAFCAELLHV K QGGGSGGG SGGGSGGGSY TDGLPAADLI PPPLKPRKVW IIYSADHPLY VDVVLKFAQF LLTACGTEVA LDLLEEQAIS EA GVMTWVG RQKQEMVESN SKIIVLCSRG TRAKWQALLG RGAPVRLRCD HGKPVGDLFT AAMNMILPDF KRPACFGTYV VCY FSEVSC DGDVPDLFGA APRYPLMDRF EEVYFRIQDL EMFQPGRMHR VGELSGDNYL RSPGGRQLRA ALDRFRDWQV RCPD WFECE NLYSADDQDA PSLDEEVFEE PLLPPGTGIV KRAPLVREPG SQACLAIDPL VGEEGGAAVA KLEPHLQPRG QPAPQ PLHT LVLAAEEGAL VAAVEPGPLA DGAAVRLALA GEGEACPLLG SPGAGRNSVL FLPVDPEDSP LGSSTPMASP DLLPED VRE HLEGLMLSLF EQSLSCQAQG GCSRPAMVLT DPHTPYEEEQ RQSVQSDQGY ISRSSPQPPE GLTEMEEEEE EEQDPGK PA LPLSPEDLES LRSLQRQLLF RQLQKNSGWD TMGSESEGPS A

UniProtKB: Interleukin-17 receptor B, Interleukin-17 receptor A

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Macromolecule #2: E3 ubiquitin ligase TRAF3IP2

MacromoleculeName: E3 ubiquitin ligase TRAF3IP2 / type: protein_or_peptide / ID: 2 / Number of copies: 15 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.936861 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GPLEAELRPQ VPQPPSPAAV PRPPSNPPAR GTLKTSNLPE ELRKVFITYS MDTAMEVVKF VNFLLVNGFQ TAIDIFEDRI RGIDIIKWM ERYLRDKTVM IIVAISPKYK QDVEGAESQL DEDEHGLHTK YIHRMMQIEF IKQGSMNFRF IPVLFPNAKK E HVPTWLQN ...String:
GPLEAELRPQ VPQPPSPAAV PRPPSNPPAR GTLKTSNLPE ELRKVFITYS MDTAMEVVKF VNFLLVNGFQ TAIDIFEDRI RGIDIIKWM ERYLRDKTVM IIVAISPKYK QDVEGAESQL DEDEHGLHTK YIHRMMQIEF IKQGSMNFRF IPVLFPNAKK E HVPTWLQN THVYSWPKNK KNILLRLLRE EEFVAPPRGP LPTLQVVPL

UniProtKB: E3 ubiquitin ligase TRAF3IP2

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Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: NITROGEN

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 157029
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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