2bph
From Proteopedia
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'''STRUCTURE OF MURINE DECTIN-1''' | '''STRUCTURE OF MURINE DECTIN-1''' | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
2BPH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPH OCA]. | 2BPH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPH OCA]. | ||
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| + | ==Reference== | ||
| + | Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function., Brown J, O'Callaghan CA, Marshall AS, Gilbert RJ, Siebold C, Gordon S, Brown GD, Jones EY, Protein Sci. 2007 Jun;16(6):1042-52. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17473009 17473009] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Fungal recognition]] | [[Category: Fungal recognition]] | ||
[[Category: Receptor]] | [[Category: Receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:20:32 2008'' |
Revision as of 19:20, 22 May 2008
STRUCTURE OF MURINE DECTIN-1
Overview
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.
About this Structure
2BPH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function., Brown J, O'Callaghan CA, Marshall AS, Gilbert RJ, Siebold C, Gordon S, Brown GD, Jones EY, Protein Sci. 2007 Jun;16(6):1042-52. Epub 2007 May 1. PMID:17473009 Page seeded by OCA on Thu May 22 22:20:32 2008
