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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 angstroms 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.

Original publication

DOI

10.1110/ps.072791207

Type

Journal article

Journal

Protein Sci

Publication Date

06/2007

Volume

16

Pages

1042 - 1052

Keywords

Animals, Cations, Divalent, Crystallography, X-Ray, Fungal Proteins, Glucans, Lectins, C-Type, Membrane Proteins, Mice, Models, Molecular, Nerve Tissue Proteins, Polysaccharides, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Receptors, Immunologic, Structure-Activity Relationship, beta-Glucans