4.6 Article

Structure of the fungal β-glucan-binding immune receptor dectin-1:: Implications for function

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

  1. MRC [G116/165] Funding Source: UKRI
  2. Medical Research Council [G116/165] Funding Source: researchfish
  3. Medical Research Council [G116/165] Funding Source: Medline
  4. Wellcome Trust [070018, 055109] Funding Source: Medline

向作者/读者索取更多资源

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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