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PDBsum entry 1q8m
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Immune system receptor
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PDB id
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1q8m
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Contents |
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* Residue conservation analysis
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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 the human myeloid cell activating receptor trem-1.
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Authors
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S.Radaev,
M.Kattah,
B.Rostro,
M.Colonna,
P.D.Sun.
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Ref.
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Structure, 2003,
11,
1527-1535.
[DOI no: ]
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PubMed id
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Abstract
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Triggering receptors expressed on myeloid cells (TREM) are a family of recently
discovered receptors that play important roles in innate immune responses, such
as to activate inflammatory responses and to contribute to septic shock in
response to microbial-mediated infections. To date, two TREM receptors in human
and several homologs in mice have been identified. We report the 2.6 A
resolution crystal structure of the extracellular domain of human TREM-1. The
overall fold of the receptor resembles that of a V-type immunoglobulin domain
with differences primarily located in the N-terminal strand. TREM-1 forms a
"head-to-tail" dimer with 4100 A(2) interface area that is partially
mediated by a domain swapping between the first strands. This mode of dimer
formation is different from the "head-to-head" dimerization that
existed in V(H)V(L) domains of antibodies or V domains of T cell receptors. As a
result, the dimeric TREM-1 most likely contains two distinct ligand binding
sites.
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Figure 2.
Figure 2. TREM-1 Dimer Interfaces(A) Stereoview of TREM-1
dimer. Secondary structure elements involved in the interactions
between N termini painted green in one monomer and yellow in
another one.(B) Detailed view of the hydrophobic core formed at
the dimer interface by the N termini of TREM-1.(C) Interactions
between CC' regions of the monomers.(D) Major interactions
holding the two dimers. Residues participating in binding are
shown as ball-and-sticks, color coded by strand color, except
for oxygen (red), nitrogen (blue), and sulfur (yellow).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
1527-1535)
copyright 2003.
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