{"entity": "publication", "iuid": "02b285ce5bce4603802f481d83ee7f79", "timestamp": "2026-10-11T08:32:47.231Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/02b285ce5bce4603802f481d83ee7f79.json"}, "display": {"href": "https://publications.scilifelab.se/publication/02b285ce5bce4603802f481d83ee7f79"}}, "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.", "authors": [{"family": "Gallego", "given": "Pablo", "initials": "P"}, {"family": "Garcia-Bonete", "given": "Maria-Jose", "initials": "MJ", "orcid": "0000-0002-8832-4338", "researcher": {"href": "https://publications.scilifelab.se/researcher/ca1f7997b83b4b2398d08c2b2a927e5e.json"}}, {"family": "Trillo-Muyo", "given": "Sergio", "initials": "S", "orcid": "0000-0002-3135-9134", "researcher": {"href": "https://publications.scilifelab.se/researcher/2e6b6b830e9145a2ae3e6c10895acbee.json"}}, {"family": "Recktenwald", "given": "Christian V", "initials": "CV", "orcid": "0000-0003-1710-1863", "researcher": {"href": "https://publications.scilifelab.se/researcher/2f82f923a04c4369aef10e6cf4e6c7f1.json"}}, {"family": "Johansson", "given": "Malin E V", "initials": "MEV", "orcid": "0000-0002-4237-6677", "researcher": {"href": "https://publications.scilifelab.se/researcher/520dab35c19049c8b3f1083a92e60d56.json"}}, {"family": "Hansson", "given": "Gunnar C", "initials": "GC", "orcid": "0000-0002-1900-1869", "researcher": {"href": "https://publications.scilifelab.se/researcher/44b3815603154322a6dac16f2fc1c1e9.json"}}], "type": "journal article", "published": "2023-04-08", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "14", "issue": "1", "pages": "1969", "issn-l": "2041-1723"}, "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 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.", "doi": "10.1038/s41467-023-37666-8", "pmid": "37031240", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC10082768"}, {"db": "pii", "key": "10.1038/s41467-023-37666-8"}], "notes": [], "created": "2023-11-28T13:06:35.939Z", "modified": "2023-11-28T13:06:36.019Z"}