2BPH

STRUCTURE OF MURINE DECTIN-1

Summary for 2BPH

• Entry DOI: 10.2210/pdb2bph/pdb
• Related: 2BPD 2BPE
• Descriptor: DECTIN-1, MAGNESIUM ION (3 entities in total)
• Functional Keywords: receptor, dectin-1, beta-glucan, fungal recognition, c-type lectin-like domain, ctld, carbohydrate
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 2
• Total formula weight: 32502.69

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: 2023-12-13)

Primary citation

Brown, 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

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)