ArticleThe FEBS journal2021
Conformational switches and redox properties of the colon cancer-associated human lectin ZG16.
Article in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 27 citations in OpenAlex.
- QSOX1: A Mysterious Golgi-Localized Disulfide Bond Catalyst and an Emerging Cancer Regulator.Cancers · 2026Article
- LncRNA HAND2-AS1 Inhibited Colon Cancer Progression By Regulating miR-3118/ZG16 Axis.Biochemical genetics · 2025Article
- Comprehensive bioinformatics analysis was used to identify and verify differentially expressed genes in targeted therapy of colon cancer.Scientific reports · 2025Article
- In Vitro Analysis of Probiotic Properties Related to the Adaptation ofInternational journal of molecular sciences · 2025Article
- PD-L1 knockout or ZG16 overexpression inhibits PDAC progression and modulates TAM polarization.Frontiers in immunology · 2025Article
- Multi-omics cluster defines the subtypes of CRC with distinct prognosis and tumor microenvironment.European journal of medical research · 2024Article
- Computational optimization of antibody humanness and stability by systematic energy-based ranking.Nature biomedical engineering · 2024Article
- Combined inhibition of histone deacetylase and cytidine deaminase improves epigenetic potency of decitabine in colorectal adenocarcinomas.Clinical epigenetics · 2023Article
- Flagella at the Host-Microbe Interface: Key Functions Intersect With Redundant Responses.Frontiers in immunology · 2022Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zymogen granule membrane protein 16 (ZG16) is produced in organs that secrete large quantities of enzymes and other proteins into the digestive tract. ZG16 binds microbial pathogens, and lower ZG16 expression levels correlate with colorectal cancer, but the physiological function of the protein is poorly understood. One prominent attribute of ZG16 is its ability to bind glycans, but other aspects of the protein may also contribute to activity. An intriguing feature of ZG16 is a CXXC motif at the carboxy terminus. Here, we describe crystal structures and biochemical studies showing that the CXXC motif is on a flexible tail, where it contributes little to structure or stability but is available to engage in redox reactions. Specifically, we demonstrate that the ZG16 cysteine thiols can be oxidized to a disulfide by quiescin sulfhydryl oxidase 1, which is a sulfhydryl oxidase present together with ZG16 in the Golgi apparatus and in mucus, as well as by protein disulfide isomerase. ZG16 crystal structures also draw attention to a nonproline cis peptide bond that can isomerize within the protein and to the mobility of glycine-rich loops in the glycan-binding site. An understanding of the properties of the ZG16 CXXC motif and the discovery of internal conformational switches extend existing knowledge relating to the glycan-binding activity of the protein.
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