Nature Communications (Apr 2023)

The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins

  • Pablo Gallego,
  • Maria-Jose Garcia-Bonete,
  • Sergio Trillo-Muyo,
  • Christian V. Recktenwald,
  • Malin E. V. Johansson,
  • Gunnar C. Hansson

DOI
https://doi.org/10.1038/s41467-023-37666-8
Journal volume & issue
Vol. 14, no. 1
pp. 1 – 9

Abstract

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The MUC2 mucin is a large, highly glycosylated polymer that builds the intestinal mucus. Here, the authors generate a high-resolution structural model of the 800 amino acid C-terminal dimer including its glycans. Stabilization is achieved by interdimer disulfide-bonds in both ends, essential for a stable mucus barrier.