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

James Brown, Chris A. O'Callaghan, Andrew S.J. Marshall, Robert J.C. Gilbert, Christian Siebold, Siamon Gordon, Gordon D. Brown, E. Yvonne Jones*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

143 Scopus citations

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 languageEnglish
Pages (from-to)1042-1052
Number of pages11
JournalProtein Science
Volume16
Issue number6
DOIs
StatePublished - 06 2007
Externally publishedYes

Keywords

  • C-type lectin-like domain
  • Fungal pathogen
  • Immune recognition
  • Protein crystallography
  • β-glucan

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