PDBsum entry 1u9k

Immune system

PDB id: 1u9k

Contents

Protein chains

110 a.a. *

Metals

_ZN ×3

Waters ×59

* Residue conservation analysis

PDB id:

1u9k

Name:

Immune system

Title:

Crystal structure of mouse triggering receptor expressed on myeloid cells 1 (trem-1) at 1.76

Structure:

Triggering receptor expressed on myeloid cells 1. Chain: a, b. Synonym: triggering receptor expressed in monocytes 1, trem-1. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: trem. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.76Å R-factor: 0.226 R-free: 0.248

Authors:

M.S.Kelker,E.W.Debler,I.A.Wilson

Key ref:

M.S.Kelker et al. (2004). Crystal structure of mouse triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.76 A. J Mol Biol, 344, 1175-1181. PubMed id: 15561137 DOI: 10.1016/j.jmb.2004.10.009

Date:

09-Aug-04 Release date: 14-Dec-04

Protein chains

Q9JKE2  (TREM1_MOUSE) -  Triggering receptor expressed on myeloid cells 1 from Mus musculus

Seq: 230 a.a.

Struc: 110 a.a.

DOI no: 10.1016/j.jmb.2004.10.009

J Mol Biol 344:1175-1181 (2004)

PubMed id: 15561137

Crystal structure of mouse triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.76 A.

M.S.Kelker, E.W.Debler, I.A.Wilson.

ABSTRACT

Triggering receptor expressed on myeloid cells (TREM) 1 is an activating receptor expressed on myeloid cells whose ligand(s) remain elusive. TREM-1 stimulation activates neutrophils and monocytes and induces the secretion of pro-inflammatory molecules, which amplifies the Toll-like receptor-initiated responses to invading pathogens. In addition, TREM-1 mediates the septic shock pathway, and thus represents a potential therapeutic target. We report the crystal structure of the mouse TREM-1 extracellular domain at 1.76A resolution. The mouse extracellular domain is monomeric, consistent with our previous human TREM-1 structure, and strongly supports the contention that the globular TREM-1 head is a monomer contrary to proposals of a symmetric dimer.

Selected figure(s)

Figure 1.
Figure 1. Stereoview of an overlay of mTREM-1 and comparison with other related immunoglobulin folds. (a) A ribbon diagram of the mTREM-1 structure determined here. (b) The mTREM-1 structure (cyan) has the expected V-set Ig domain fold seen in immunoglobulins (light blue, PDB code 1mfa), T-cell receptors (green, PDB code 1tcr) and the human natural killer cell activating receptor, NKp44 (red, PDB code 1hkf). The groove formed by b-hairpins formed by strands C-C' and F-G is more pronounced than those in IgG, TCR or activating receptor Ig domains. Furthermore, mTREM-1 lacks the disulfide bridge (C37-C45) present only in NKp44. (c) Stereoview of a C^a trace of the previously published hTREM-1 structures from our laboratory (blue, 1smo),15 Radeav et al.14 (1q8m, green), and our mTREM-1 structure (red). The orientation mTREM-1 overlays in b) and c) are identical with that in a). Disulfides are labeled yellow (for carbon) and green (for sulfur). This Figure, and all subsequent ribbon diagrams, were made with Bobscript22 and Raster3D.23

Figure 3.
Figure 3. Electrostatic surface potential and conservation of surface residues of mTREM-1. Left: the surfaces and electrostatic potentials were generated in INSIGHTII (Molecular Simulations, Inc., San Diego, CA). Positive potential (>=10 mV) is blue, neutral potential (0 mV) is white and negative potential ( -10 mV) is red. CDR-equivalent regions are marked by an oval. Right: Accessible surface area representation and ribbon diagram of the mTREM-1 Ig domain was generated using PyMOL (http://pymol.sourceforge.net/). Residues with 100% identity between the human, mouse, cow and pig TREM-1 sequences are colored green. The "Front" orientation is equivalent to that of Figure 1(a).

The above figures are reprinted by permission from Elsevier: J Mol Biol (2004, 344, 1175-1181) copyright 2004.

Figures were selected by an automated process.