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

¹ CR-UK Receptor Structure Research Group, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, United Kingdom
² Henry Wellcome Building of Molecular Physiology, Oxford, OX3 7BN, United Kingdom
³ Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom
⁴ Institute of Infectious Disease and Molecular Medicine, CLS, Faculty of Health Sciences, University of Cape Town, Observatory, 7925, Cape Town, South Africa

(RECEIVED January 26, 2007; FINAL REVISION March 19, 2007; ACCEPTED March 20, 2007)

The murine molecule dectin-1 (known as the -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 -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 -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 -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.

Keywords: immune recognition; fungal pathogen; -glucan; protein crystallography; C-type lectin-like domain

Abbreviations: AUC, analytical ultracentrifugation; GR, human -glucan receptor; BGC, -glucan; CTLD, C-type lectin-like domain; DLS, dynamic light scattering; TTX, Triton X-100.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.072791207.

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