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PDBsum entry 1t8d
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Immune system
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PDB id
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1t8d
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Contents |
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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Structure of thE C-type lectin domain of cd23
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Structure:
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Low affinity immunoglobulin epsilon fc receptor. Chain: a. Fragment: dercd23. Synonym: lymphocyte ige receptor, fc-epsilon-rii, cd23, immunoglobulin e-binding factor. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: fcer2, igebf. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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NMR struc:
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20 models
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Authors:
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R.G.Hibbert,P.Teriete,G.J.Grundy,B.J.Sutton,H.J.Gould,J.M.Mcdonnell
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Key ref:
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R.G.Hibbert
et al.
(2005).
The structure of human CD23 and its interactions with IgE and CD21.
J Exp Med,
202,
751-760.
PubMed id:
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Date:
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12-May-04
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Release date:
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26-Jul-05
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PROCHECK
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Headers
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References
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P06734
(FCER2_HUMAN) -
Low affinity immunoglobulin epsilon Fc receptor from Homo sapiens
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Seq:
Struc:
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321 a.a.
143 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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J Exp Med
202:751-760
(2005)
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PubMed id:
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The structure of human CD23 and its interactions with IgE and CD21.
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R.G.Hibbert,
P.Teriete,
G.J.Grundy,
R.L.Beavil,
R.Reljic,
V.M.Holers,
J.P.Hannan,
B.J.Sutton,
H.J.Gould,
J.M.McDonnell.
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ABSTRACT
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The low-affinity immunoglobulin E (IgE) receptor, CD23 (FcepsilonRII), binds
both IgE and CD21 and, through these interactions, regulates the synthesis of
IgE, the antibody isotype that mediates the allergic response. We have
determined the three-dimensional structure of the C-type lectin domain of CD23
in solution by nuclear magnetic resonance spectroscopy. An analysis of
concentration-dependent chemical shift perturbations have allowed us to identify
the residues engaged in self-association to the trimeric state, whereas
ligand-induced changes have defined the binding sites for IgE and CD21. The
results further reveal that CD23 can bind both ligands simultaneously. Despite
the C-type lectin domain structure, none of the interactions require calcium. We
also find that IgE and CD23 can interact to form high molecular mass multimeric
complexes. The interactions that we have described provide a solution to the
paradox that CD23 is involved in both up- and down-regulation of IgE and provide
a structural basis for the development of inhibitors of allergic disease.
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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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B.Steiniger,
M.Trabandt,
and
P.J.Barth
(2011).
The follicular dendritic cell network in secondary follicles of human palatine tonsils and spleens.
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Histochem Cell Biol,
135,
327-336.
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L.E.Cheng,
Z.E.Wang,
and
R.M.Locksley
(2010).
Murine B cells regulate serum IgE levels in a CD23-dependent manner.
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J Immunol,
185,
5040-5047.
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L.Tang,
J.Yang,
X.Tang,
W.Ying,
X.Qian,
and
F.He
(2010).
The DC-SIGN family member LSECtin is a novel ligand of CD44 on activated T cells.
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Eur J Immunol,
40,
1185-1191.
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M.Acharya,
G.Borland,
A.L.Edkins,
L.M.Maclellan,
J.Matheson,
B.W.Ozanne,
and
W.Cushley
(2010).
CD23/FcεRII: molecular multi-tasking.
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Clin Exp Immunol,
162,
12-23.
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D.Veneri,
R.Ortolani,
M.Franchini,
G.Tridente,
G.Pizzolo,
and
A.Vella
(2009).
Expression of CD27 and CD23 on peripheral blood B lymphocytes in humans of different ages.
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Blood Transfus,
7,
29-34.
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L.Jackson,
C.T.Cady,
and
J.C.Cambier
(2009).
TLR4-mediated signaling induces MMP9-dependent cleavage of B cell surface CD23.
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J Immunol,
183,
2585-2592.
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L.Tang,
J.Yang,
W.Liu,
X.Tang,
J.Chen,
D.Zhao,
M.Wang,
F.Xu,
Y.Lu,
B.Liu,
Q.Sun,
L.Zhang,
and
F.He
(2009).
Liver sinusoidal endothelial cell lectin, LSECtin, negatively regulates hepatic T-cell immune response.
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Gastroenterology,
137,
1498.
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M.Buc,
M.Dzurilla,
M.Vrlik,
and
M.Bucova
(2009).
Immunopathogenesis of bronchial asthma.
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Arch Immunol Ther Exp (Warsz),
57,
331-344.
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M.D.Knolle,
and
C.A.Owen
(2009).
ADAM8: a new therapeutic target for asthma.
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Expert Opin Ther Targets,
13,
523-540.
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P.N.Mwinzi,
L.Ganley-Leal,
C.L.Black,
W.E.Secor,
D.M.Karanja,
and
D.G.Colley
(2009).
Circulating CD23+ B cell subset correlates with the development of resistance to Schistosoma mansoni reinfection in occupationally exposed adults who have undergone multiple treatments.
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J Infect Dis,
199,
272-279.
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F.Shakib,
A.M.Ghaemmaghami,
and
H.F.Sewell
(2008).
The molecular basis of allergenicity.
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Trends Immunol,
29,
633-642.
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H.J.Gould,
and
B.J.Sutton
(2008).
IgE in allergy and asthma today.
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Nat Rev Immunol,
8,
205-217.
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D.H.Conrad,
J.W.Ford,
J.L.Sturgill,
and
D.R.Gibb
(2007).
CD23: an overlooked regulator of allergic disease.
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Curr Allergy Asthma Rep,
7,
331-337.
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G.A.Lemieux,
F.Blumenkron,
N.Yeung,
P.Zhou,
J.Williams,
A.C.Grammer,
R.Petrovich,
P.E.Lipsky,
M.L.Moss,
and
Z.Werb
(2007).
The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase ADAM10.
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J Biol Chem,
282,
14836-14844.
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M.Zhang,
R.F.Murphy,
and
D.K.Agrawal
(2007).
Decoding IgE Fc receptors.
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Immunol Res,
37,
1.
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R.Furmonaviciene,
A.M.Ghaemmaghami,
S.E.Boyd,
N.S.Jones,
K.Bailey,
A.C.Willis,
H.F.Sewell,
D.A.Mitchell,
and
F.Shakib
(2007).
The protease allergen Der p 1 cleaves cell surface DC-SIGN and DC-SIGNR: experimental analysis of in silico substrate identification and implications in allergic responses.
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Clin Exp Allergy,
37,
231-242.
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B.A.Wurzburg,
S.S.Tarchevskaya,
and
T.S.Jardetzky
(2006).
Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding.
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Structure,
14,
1049-1058.
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PDB codes:
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P.D.Sun
(2006).
Human CD23: is it a lectin in disguise?
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Structure,
14,
950-951.
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R.L.Rich,
and
D.G.Myszka
(2006).
Survey of the year 2005 commercial optical biosensor literature.
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J Mol Recognit,
19,
478-534.
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A.N.Zelensky,
and
J.E.Gready
(2005).
The C-type lectin-like domain superfamily.
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FEBS J,
272,
6179-6217.
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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
