ArticleThe FEBS journal2025
The structure of FCGBP is formed as a disulfide-mediated homodimer between its C-terminal domains.
Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- The tumor-suppressive function of the unique H domain of FCGBP and its potential as a therapeutic target in colorectal cancer.BMC cancer · 2026Article
- FCGBP links hormonal imbalance and hepatic steatosis in PCOS-NAFLD comorbidity: an integrative bioinformatics and experimental study.Frontiers in endocrinology · 2026Article
- FCGBP promotes ovarian cancer progression via activation of IL-6/JAK-STAT signaling pathway.Journal of translational medicine · 2025Article
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Authors and funding
7 authors.
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Abstract
Mucus in the colon is crucial for intestinal homeostasis by forming a barrier that separates microbes from the epithelium. This is achieved by the structural arrangement of the major mucus proteins, such as MUC2 and FCGBP, both of which are comprised of several von Willebrand D domains (vWD) and assemblies. Numerous disulfide bonds stabilise these domains, and intermolecular bonds generate multimers of MUC2. The oligomeric nature of FCGBP is not known. Human hFCGBP contains 13 vWD domains whereas mouse mFCGBP consists of only 7. We found unpaired cysteines in the vWD1 (human and mouse) and vWD5 (mouse)/vWD11 (human) assemblies which were not involved in disulfide bonds. However, the most C-terminal vWD domains, vWD7 (mouse)/vWD13 (human), formed disulfide-linked dimers. The intermolecular bond between C
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