The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins
oleh: Pablo Gallego, Maria-Jose Garcia-Bonete, Sergio Trillo-Muyo, Christian V. Recktenwald, Malin E. V. Johansson, Gunnar C. Hansson
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2023-04-01 |
Deskripsi
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.