7qcu
Structure of the MUCIN-2 Cterminal domains partially deglycosylated.
Structural highlights
FunctionMUC2_HUMAN Coats the epithelia of the intestines, airways, and other mucus membrane-containing organs. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. Major constituent of both the inner and outer mucus layers of the colon and may play a role in excluding bacteria from the inner mucus layer.[1] Publication Abstract from PubMedThe 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. The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins.,Gallego P, Garcia-Bonete MJ, Trillo-Muyo S, Recktenwald CV, Johansson MEV, Hansson GC Nat Commun. 2023 Apr 8;14(1):1969. doi: 10.1038/s41467-023-37666-8. PMID:37031240[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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