2BPE
STRUCTURE OF MURINE DECTIN-1
Summary for 2BPE
Entry DOI | 10.2210/pdb2bpe/pdb |
Related | 2BPD 2BPH |
Descriptor | DECTIN-1, CALCIUM ION, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | receptor, dectin-1, beta-glucan, fungal recognition, c-type lectin-like domain, ctld |
Biological source | MUS MUSCULUS (MOUSE) |
Total number of polymer chains | 2 |
Total formula weight | 33064.50 |
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 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 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: 17473009DOI: 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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