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...
Main Authors: | , , , , , , , |
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Format: | Journal article |
Language: | English |
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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. |
first_indexed | 2024-03-06T21:20:27Z |
format | Journal article |
id | oxford-uuid:41450ed8-f3c9-46d0-92a9-a51be7b05f11 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T21:20:27Z |
publishDate | 2007 |
record_format | dspace |
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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