2cl8

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{{STRUCTURE_2cl8| PDB=2cl8 | SCENE= }}
{{STRUCTURE_2cl8| PDB=2cl8 | SCENE= }}
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'''DECTIN-1 IN COMPLEX WITH BETA-GLUCAN'''
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===DECTIN-1 IN COMPLEX WITH BETA-GLUCAN===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 17473009 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17473009}}
==About this Structure==
==About this Structure==
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[[Category: Laminarin]]
[[Category: Laminarin]]
[[Category: Receptor]]
[[Category: Receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:38:32 2008''

Revision as of 21:38, 27 July 2008

Template:STRUCTURE 2cl8

DECTIN-1 IN COMPLEX WITH BETA-GLUCAN

Template:ABSTRACT PUBMED 17473009

About this Structure

2CL8 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

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