6V1C

Crystal structure of human trefoil factor 3 in complex with its cognate ligand

6V1C の概要

• エントリーDOI: 10.2210/pdb6v1c/pdb
• 分子名称: Trefoil factor 3, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-beta-D-galactopyranose (3 entities in total)
• 機能のキーワード: trefoil factor, lectin, mucin binding protein, sugar binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7287.20

構造登録者

Jarva, M.A.,Lingford, J.P.,John, A.,Scott, N.E.,Goddard-Borger, E.D. (登録日: 2019-11-20, 公開日: 2019-12-11, 最終更新日: 2023-10-11)

主引用文献

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

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: 32404934
DOI: 10.1038/s41467-020-16223-7

実験手法

X-RAY DIFFRACTION (1.55 Å)