Abstract
The murine molecule dectin-1 (known as the β-glucan receptor in humans) is an immune cell surface receptor implicated in the immunological defense against fungal pathogens. Sequence analysis has indicated that the dectin-1 extracellular domain is a C-type lectin-like domain, and functional studies have established that it binds fungal β-glucans. We report several dectin-1 crystal structures, including a high-resolution structure and a 2.8 Å resolution structure in which a short soaked natural β-glucan is trapped in the crystal lattice. In vitro characterization of dectin-1 in the presence of its natural ligand indicates higher-order complex formation between dectin-1 and β-glucans. These combined structural and biophysical data considerably extend the current knowledge of dectin-1 structure and function, and suggest potential mechanisms of defense against fungal pathogens. Published by Cold Spring Harbor Laboratory Press.
Original language | English |
---|---|
Pages (from-to) | 1042-1052 |
Number of pages | 11 |
Journal | Protein Science |
Volume | 16 |
Issue number | 6 |
DOIs | |
State | Published - 06 2007 |
Externally published | Yes |
Keywords
- C-type lectin-like domain
- Fungal pathogen
- Immune recognition
- Protein crystallography
- β-glucan