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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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TRAF6 coiled-coil domain mediates its trimerization.

Mohammed Khan1, Rui Yang1, Qian Yin1,2

  • 1Department of Biological Science, Florida State University, Tallahassee, FL 32306.

Biorxiv : the Preprint Server for Biology
|January 9, 2026
PubMed
Summary
This summary is machine-generated.

Tumor necrosis factor receptor-associated factor 6 (TRAF6) coiled-coil domain forms a trimer, as confirmed by experimental and computational methods. This finding provides structural insights into TRAF6 assembly in innate immunity signaling.

Keywords:
TRAF6coiled-coil domainoligomerizationtrimerization

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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
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Area of Science:

  • Molecular Biology
  • Immunology
  • Structural Biology

Background:

  • TRAF6 is a crucial adaptor protein in innate immune signaling.
  • Its coiled-coil domain's oligomeric state is largely uncharacterized.
  • Understanding TRAF6 structure is key to its function in immune pathways.

Purpose of the Study:

  • To determine the oligomeric state of the human TRAF6 coiled-coil domain.
  • To provide experimental and computational evidence for its structural assembly.
  • To establish a framework for TRAF6 higher-order structure formation.

Main Methods:

  • Size-exclusion chromatography (SEC) and SEC-multi-angle light scattering (SEC-MALS) were used.
  • Coiled-coil computational prediction tools were employed.
  • AlphaFold-Multimer modeling was utilized for structural analysis.

Main Results:

  • Both His-tagged and tagless TRAF6 coiled-coil domains consistently showed a trimeric molecular mass.
  • Computational analysis revealed a heptad repeat pattern supporting trimerization.
  • AlphaFold-Multimer modeling predicted a symmetric trimer with a hydrophobic core.

Conclusions:

  • Experimental data strongly support the trimerization of the TRAF6 coiled-coil domain.
  • These findings offer a structural basis for TRAF6 assembly into functional complexes.
  • This work advances the understanding of TRAF6's role in innate immunity.