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PDBsum entry 1hkf
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Contents |
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* Residue conservation analysis
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PDB id:
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Receptor
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Title:
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The three dimensional structure of nk cell receptor nkp44, a triggering partner in natural cytotoxicity
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Structure:
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Nk cell activating receptor. Chain: a. Fragment: ig domain, residues 19-130. Synonym: nkp44. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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2.20Å
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R-factor:
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0.240
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R-free:
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0.245
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Authors:
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M.Ponassi,C.Cantoni,R.Biassoni,R.Conte,A.Spallarossa,A.Moretta, L.Moretta,M.Bolognesi,D.Bordo
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Key ref:
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C.Cantoni
et al.
(2003).
The three-dimensional structure of the human NK cell receptor NKp44, a triggering partner in natural cytotoxicity.
Structure,
11,
725-734.
PubMed id:
DOI:
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Date:
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10-Mar-03
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Release date:
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11-Jun-03
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PROCHECK
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Headers
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References
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O95944
(NCTR2_HUMAN) -
Natural cytotoxicity triggering receptor 2 from Homo sapiens
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Seq:
Struc:
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276 a.a.
108 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Structure
11:725-734
(2003)
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PubMed id:
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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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C.Cantoni,
M.Ponassi,
R.Biassoni,
R.Conte,
A.Spallarossa,
A.Moretta,
L.Moretta,
M.Bolognesi,
D.Bordo.
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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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Selected figure(s)
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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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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.E.Ostergaard,
K.P.Lubieniecki,
S.A.Martin,
R.J.Stet,
W.S.Davidson,
and
C.J.Secombes
(2010).
Genomic organisation analysis of novel immunoglobulin-like transcripts in Atlantic salmon (Salmo salar) reveals a tightly clustered and multigene family.
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BMC Genomics,
11,
697.
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A.De Maria,
E.Ugolotti,
E.Rutjens,
S.Mazza,
L.Radic,
A.Faravelli,
G.Koopman,
E.Di Marco,
P.Costa,
B.Ensoli,
A.Cafaro,
M.C.Mingari,
L.Moretta,
J.Heeney,
and
R.Biassoni
(2009).
NKp44 expression, phylogenesis and function in non-human primate NK cells.
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Int Immunol,
21,
245-255.
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H.R.Kim,
K.H.Lee,
S.J.Park,
S.Y.Kim,
Y.K.Yang,
J.Tae,
and
J.Kim
(2009).
Anti-cancer activity and mechanistic features of a NK cell activating molecule.
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Cancer Immunol Immunother,
58,
1691-1700.
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J.A.Doebbler,
and
R.B.Von Dreele
(2009).
Application of molecular replacement to protein powder data from image plates.
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Acta Crystallogr D Biol Crystallogr,
65,
348-355.
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O.Hershkovitz,
B.Rosental,
L.A.Rosenberg,
M.E.Navarro-Sanchez,
S.Jivov,
A.Zilka,
O.Gershoni-Yahalom,
E.Brient-Litzler,
H.Bedouelle,
J.W.Ho,
K.S.Campbell,
B.Rager-Zisman,
P.Despres,
and
A.Porgador
(2009).
NKp44 receptor mediates interaction of the envelope glycoproteins from the West Nile and dengue viruses with NK cells.
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J Immunol,
183,
2610-2621.
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J.P.Cannon,
R.N.Haire,
A.T.Magis,
D.D.Eason,
K.N.Winfrey,
J.A.Hernandez Prada,
K.M.Bailey,
J.Jakoncic,
G.W.Litman,
and
D.A.Ostrov
(2008).
A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition.
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Immunity,
29,
228-237.
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PDB codes:
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M.A.Zhuravleva,
K.Trandem,
and
P.D.Sun
(2008).
Structural implications of Siglec-5-mediated sialoglycan recognition.
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J Mol Biol,
375,
437-447.
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PDB codes:
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T.I.Arnon,
J.T.Kaiser,
A.P.West,
R.Olson,
R.Diskin,
B.C.Viertlboeck,
T.W.Göbel,
and
P.J.Bjorkman
(2008).
The crystal structure of CHIR-AB1: a primordial avian classical Fc receptor.
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J Mol Biol,
381,
1012-1024.
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PDB code:
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G.W.Litman,
J.P.Cannon,
L.J.Dishaw,
R.N.Haire,
D.D.Eason,
J.A.Yoder,
J.H.Prada,
and
D.A.Ostrov
(2007).
Immunoglobulin variable regions in molecules exhibiting characteristics of innate and adaptive immune receptors.
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Immunol Res,
38,
294-304.
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B.C.Viertlboeck,
R.Schmitt,
and
T.W.Göbel
(2006).
The chicken immunoregulatory receptor families SIRP, TREM, and CMRF35/CD300L.
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Immunogenetics,
58,
180-190.
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J.P.Cannon,
R.N.Haire,
M.G.Mueller,
R.T.Litman,
D.D.Eason,
D.Tinnemore,
C.T.Amemiya,
T.Ota,
and
G.W.Litman
(2006).
Ancient divergence of a complex family of immune-type receptor genes.
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Immunogenetics,
58,
362-373.
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T.I.Arnon,
G.Markel,
and
O.Mandelboim
(2006).
Tumor and viral recognition by natural killer cells receptors.
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Semin Cancer Biol,
16,
348-358.
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Y.T.Bryceson,
M.E.March,
H.G.Ljunggren,
and
E.O.Long
(2006).
Synergy among receptors on resting NK cells for the activation of natural cytotoxicity and cytokine secretion.
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Blood,
107,
159-166.
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R.J.Stet,
T.Hermsen,
A.H.Westphal,
J.Jukes,
M.Engelsma,
B.M.Lidy Verburg-van Kemenade,
J.Dortmans,
J.Aveiro,
and
H.F.Savelkoul
(2005).
Novel immunoglobulin-like transcripts in teleost fish encode polymorphic receptors with cytoplasmic ITAM or ITIM and a new structural Ig domain similar to the natural cytotoxicity receptor NKp44.
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Immunogenetics,
57,
77-89.
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R.Biassoni,
C.Cantoni,
D.Marras,
J.Giron-Michel,
M.Falco,
L.Moretta,
and
N.Dimasi
(2003).
Human natural killer cell receptors: insights into their molecular function and structure.
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J Cell Mol Med,
7,
376-387.
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S.Radaev,
M.Kattah,
B.Rostro,
M.Colonna,
and
P.D.Sun
(2003).
Crystal structure of the human myeloid cell activating receptor TREM-1.
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Structure,
11,
1527-1535.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
