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Title | The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 1969, Year 2023 |
Publish date | Apr 8, 2023 |
Authors | Pablo Gallego / Maria-Jose Garcia-Bonete / Sergio Trillo-Muyo / Christian V Recktenwald / Malin E V Johansson / Gunnar C Hansson / |
PubMed Abstract | The MUC2 mucin polymer is the main building unit of the intestinal mucus layers separating intestinal microbiota from the host epithelium. The MUC2 mucin is a large glycoprotein with a C-terminal ...The MUC2 mucin polymer is the main building unit of the intestinal mucus layers separating intestinal microbiota from the host epithelium. The MUC2 mucin is a large glycoprotein with a C-terminal domain similar to the MUC5AC and MUC5B mucins and the von Willebrand factor (VWF). A structural model of the C-terminal part of MUC2, MUC2-C, was generated by combining Cryo-electron microscopy, AlphaFold prediction, information of its glycosylation, and small angle X-ray scattering information. The globular VWD4 assembly in the N-terminal of MUC2-C is followed by 3.5 linear VWC domains that form an extended flexible structure before the C-terminal cystine-knot. All gel-forming mucins and VWF form tail-tail disulfide-bonded dimers in their C-terminal cystine-knot domain, but interestingly the MUC2 mucin has an extra stabilizing disulfide bond on the N-terminal side of the VWD4 domain, likely essential for a stable intestinal mucus barrier. |
External links | Nat Commun / PubMed:37031240 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.25 - 3.4 Å |
Structure data | EMDB-13896, PDB-7qcl: EMDB-13897, PDB-7qcn: EMDB-13899, PDB-7qcu: |
Chemicals | ChemComp-NAG: ChemComp-CA: |
Source |
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Keywords | STRUCTURAL PROTEIN / Mucus / extracellular / net assemble |