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PDBsum entry 1u9k
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Immune system
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PDB id
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1u9k
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References listed in PDB file
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Key reference
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Title
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Crystal structure of mouse triggering receptor expressed on myeloid cells 1 (trem-1) at 1.76 a.
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Authors
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M.S.Kelker,
E.W.Debler,
I.A.Wilson.
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Ref.
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J Mol Biol, 2004,
344,
1175-1181.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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
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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).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2004,
344,
1175-1181)
copyright 2004.
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