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Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.


ABSTRACT: 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.

SUBMITTER: Brown J 

PROVIDER: S-EPMC2206667 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature

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Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.

Brown James J   O'Callaghan Chris A CA   Marshall Andrew S J AS   Gilbert Robert J C RJ   Siebold Christian C   Gordon Siamon S   Brown Gordon D GD   Jones E Yvonne EY  

Protein science : a publication of the Protein Society 20070501 6


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 soa  ...[more]

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