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PDBsum entry 1hkf
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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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The three-Dimensional structure of the human nk cell receptor nkp44, A triggering partner in natural cytotoxicity.
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Authors
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C.Cantoni,
M.Ponassi,
R.Biassoni,
R.Conte,
A.Spallarossa,
A.Moretta,
L.Moretta,
M.Bolognesi,
D.Bordo.
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Ref.
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Structure, 2003,
11,
725-734.
[DOI no: ]
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PubMed id
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Abstract
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Natural killer (NK) cells direct cytotoxicity against tumor or virally infected
cells. NK cell activation depends on a fine balance between inhibitory and
activating receptors. NKp44 is a cytotoxicity activating receptor composed of
one Ig-like extracellular domain, a transmembrane segment, and a cytoplasmic
domain. The 2.2 A crystal structure shows that the NKp44 Ig domain forms a
saddle-shaped dimer, where a charged surface groove protrudes from the core
structure in each subunit. NKp44 Ig domain disulfide bridge topology defines a
new Ig structural subfamily. The data presented are a first step toward
understanding the molecular basis for ligand recognition by natural cytotoxicity
receptors, whose key role in the immune system is established, but whose
cellular ligands are still elusive.
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Figure 3.
Figure 3. Superposition of NKp44 Ig Domain with the Closest
Structural HomologsTCR a chain (A), CD8 (B), and N-terminal
sialoadhesin (C) Ig domains. NKp44 is shown in gray, with the
CC' and FG loops shown in red as in Figure 1; TCR, CD8, and
sialoadhesin are shown in green, pink, and blue, respectively.
In all three drawings, the orientation of the NKp44 Ig domain is
the same as in Figure 1. Optimal superposition was performed
using the program HOMOMGRPA (Rossmann and Argos, 1976).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
725-734)
copyright 2003.
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