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A first structural model for covalent dimerization of S100 proteins.

Maria Demou1, Laure Yatime1

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|April 14, 2026
PubMed
Summary

Extracellular S100 proteins, acting as alarmins, can form covalent dimers through cysteine linkages. This study reveals a specific S100A6 dimer structure stabilized by a Cys84-Cys84 bond, compatible with receptor for advanced glycation end-products (RAGE) binding.

Keywords:
RAGE receptorsS100 proteinscovalent homodimerizationcysteinesdisulfide crosslinking

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Extracellular S100 proteins function as alarmins, initiating inflammatory responses via receptors like RAGE.
  • Oxidative environments promote S100 post-translational modifications, including disulfide bonds, forming covalent species.
  • The structure and RAGE-binding impact of these S100 covalent assemblies are poorly understood.

Purpose of the Study:

  • To investigate the molecular architecture of S100 covalent assemblies.
  • To determine the role of cysteine residues, particularly at position 84, in S100-RAGE interactions.
  • To propose a model for S100 covalent homodimerization compatible with RAGE binding.

Main Methods:

  • Bioinformatic analysis of S100 cysteine conservation.
  • Site-directed mutagenesis to introduce cysteine at S100A6 position 84.
  • SDS-PAGE under nonreducing conditions to detect covalent dimers.
  • Structural analysis of S100A6-RAGE ectodomain complex.

Main Results:

  • Cysteine residues are enriched in helix H4 of S100 proteins, with a hotspot at position 84.
  • S100A6 with a cysteine at Y84 forms a stable covalent dimer in solution.
  • Structural analysis revealed a Cys84-Cys84 linkage stabilizing the dimeric conformation of RAGE-bound S100A6.
  • Modeling suggests this covalent dimer architecture may apply to other S100 family members.

Conclusions:

  • A specific S100A6 covalent homodimer architecture involving a Cys84-Cys84 linkage has been identified.
  • This covalent dimerization mechanism is compatible with binding to the receptor for advanced glycation end-products (RAGE).
  • The findings provide a foundational model for understanding disulfide-crosslinked S100 species in inflammation.