6V1C
Crystal structure of human trefoil factor 3 in complex with its cognate ligand
Summary for 6V1C
| Entry DOI | 10.2210/pdb6v1c/pdb |
| Descriptor | Trefoil factor 3, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-beta-D-galactopyranose (3 entities in total) |
| Functional Keywords | trefoil factor, lectin, mucin binding protein, sugar binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 7287.20 |
| Authors | Jarva, M.A.,Lingford, J.P.,John, A.,Scott, N.E.,Goddard-Borger, E.D. (deposition date: 2019-11-20, release date: 2019-12-11, Last modification date: 2023-10-11) |
| Primary citation | Jarva, M.A.,Lingford, J.P.,John, A.,Soler, N.M.,Scott, N.E.,Goddard-Borger, E.D. Trefoil factors share a lectin activity that defines their role in mucus. Nat Commun, 11:2265-2265, 2020 Cited by PubMed Abstract: The mucosal epithelium secretes a host of protective disulfide-rich peptides, including the trefoil factors (TFFs). The TFFs increase the viscoelasticity of the mucosa and promote cell migration, though the molecular mechanisms underlying these functions have remained poorly defined. Here, we demonstrate that all TFFs are divalent lectins that recognise the GlcNAc-α-1,4-Gal disaccharide, which terminates some mucin-like O-glycans. Degradation of this disaccharide by a glycoside hydrolase abrogates TFF binding to mucins. Structural, mutagenic and biophysical data provide insights into how the TFFs recognise this disaccharide and rationalise their ability to modulate the physical properties of mucus across different pH ranges. These data reveal that TFF activity is dependent on the glycosylation state of mucosal glycoproteins and alludes to a lectin function for trefoil domains in other human proteins. PubMed: 32404934DOI: 10.1038/s41467-020-16223-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
Download full validation report
