PDBsum entry 2bpd

Receptor

PDB id: 2bpd

Contents

Protein chains

127 a.a. *

Waters ×436

* Residue conservation analysis

PDB id:

2bpd

Name:

Receptor

Title:

Structure of murine dectin-1

Structure:

Dectin-1. Chain: a, b. Fragment: extracellular beta-glucan recognition domain, residues 113- 244. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Cell_line: raw264.7. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta.

Biol. unit:

Dimer (from PDB file)

Resolution:

1.50Å R-factor: 0.216 R-free: 0.270

Authors:

J.Brown,C.A.O'Callaghan,A.S.J.Marshall,R.J.C.Gilbert,C.Siebold, S.Gordon,G.D.Brown,E.Y.Jones

Key ref:

J.Brown et al. (2007). Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function. Protein Sci, 16, 1042-1052. PubMed id: 17473009 DOI: 10.1110/ps.072791207

Date:

19-Apr-05 Release date: 30-Aug-06

Protein chains

Q6QLQ4  (CLC7A_MOUSE) -  C-type lectin domain family 7 member A from Mus musculus

Seq: 244 a.a.

Struc: 127 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1110/ps.072791207

Protein Sci 16:1042-1052 (2007)

PubMed id: 17473009

Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.

J.Brown, C.A.O'Callaghan, A.S.Marshall, R.J.Gilbert, C.Siebold, S.Gordon, G.D.Brown, E.Y.Jones.

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.

Selected figure(s)

Figure 3.
Figure 3. Metal ion binding coordination in dectin-1. Ball-and-stick diagram showing the octahedral metal ion coordination in dectin-1. The distances between the calcium ion and the chelating atoms are as follows: Lys156 O, 2.3 Å; Asp158 OD2, 2.2 Å; Glu162 OE1, 2.2 Å; Glu241 OE1, 2.3 Å; HOH1, 2.2 Å; and HOH2, 2.4 Å.

Figure 5.
Figure 5. Two dectin-1 monomers form a dimer into which a short -glucan binds. (A) A cartoon diagram of the dectin-1 P3[2]21 dimer, with each monomer colored from blue at the N terminus to red at the C terminus. Disulphide linkages are shown as gray balls-and-sticks, the metal ion as a golden sphere, and the bound -glucan as yellow and red balls-and-sticks. (B) Equivalent orientation as A, showing the electrostatic potential surface of the dectin-1 P3[2]21 dimer around the region where -glucan is observed, produced using GRASP and contoured ±20 kT (blue denotes positive; red, negative potential). Bound -glucan is shown as yellow and red balls-and-sticks. (C) Electron density for laminaritriose observed in a 2F[o]–F[c] composite-omit map contoured at 1 .

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2007, 16, 1042-1052) copyright 2007.

Figures were selected by an automated process.