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

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 studie...

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Main Authors: Brown, J, O'Callaghan, C, Marshall, A, Gilbert, R, Siebold, C, Gordon, S, Brown, G, Jones, E
Format: Journal article
Language:English
Published: 2007
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author Brown, J
O'Callaghan, C
Marshall, A
Gilbert, R
Siebold, C
Gordon, S
Brown, G
Jones, E
author_facet Brown, J
O'Callaghan, C
Marshall, A
Gilbert, R
Siebold, C
Gordon, S
Brown, G
Jones, E
author_sort Brown, J
collection OXFORD
description 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.
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spelling oxford-uuid:41450ed8-f3c9-46d0-92a9-a51be7b05f112022-03-26T14:42:37ZStructure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:41450ed8-f3c9-46d0-92a9-a51be7b05f11EnglishSymplectic Elements at Oxford2007Brown, JO'Callaghan, CMarshall, AGilbert, RSiebold, CGordon, SBrown, GJones, EThe 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.
spellingShingle Brown, J
O'Callaghan, C
Marshall, A
Gilbert, R
Siebold, C
Gordon, S
Brown, G
Jones, E
Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.
title Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.
title_full Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.
title_fullStr Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.
title_full_unstemmed Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.
title_short Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.
title_sort structure of the fungal beta glucan binding immune receptor dectin 1 implications for function
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