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2BPE

STRUCTURE OF MURINE DECTIN-1

Summary for 2BPE
Entry DOI10.2210/pdb2bpe/pdb
Related2BPD 2BPH
DescriptorDECTIN-1, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsreceptor, dectin-1, beta-glucan, fungal recognition, c-type lectin-like domain, ctld
Biological sourceMUS MUSCULUS (MOUSE)
Total number of polymer chains2
Total formula weight33064.50
Authors
Brown, J.,O'Callaghan, C.A.,Marshall, A.S.J.,Gilbert, R.J.C.,Siebold, C.,Gordon, S.,Brown, G.D.,Jones, E.Y. (deposition date: 2005-04-19, release date: 2006-08-31, Last modification date: 2024-11-20)
Primary citationBrown, J.,O'Callaghan, C.A.,Marshall, A.S.J.,Gilbert, R.J.C.,Siebold, C.,Gordon, S.,Brown, G.D.,Jones, E.Y.
Structure of the Fungal Beta-Glucan-Binding Immune Receptor Dectin-1: Implications for Function.
Protein Sci., 16:1042-, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17473009
DOI: 10.1110/PS.072791207
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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