期刊
PROTEIN SCIENCE
卷 16, 期 6, 页码 1042-1052出版社
WILEY
DOI: 10.1110/ps.072791207
关键词
immune recognition; fungal pathogen; beta-glucan; protein crystallography; C-type lectin-like domain
资金
- MRC [G116/165] Funding Source: UKRI
- Medical Research Council [G116/165] Funding Source: researchfish
- Medical Research Council [G116/165] Funding Source: Medline
- Wellcome Trust [070018, 055109] Funding Source: Medline
The murine molecule dectin-1 (known as the beta-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 beta-glucans. We report several dectin-1 crystal structures, including a high-resolution structure and a 2.8 angstrom resolution structure in which a short soaked natural beta-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 beta-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.
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