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Contents |
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203 a.a.
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239 a.a.
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212 a.a.
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222 a.a.
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* Residue conservation analysis
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PDB id:
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Complex (immunoreceptor/immunoglobulin)
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Title:
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An alpha-beta t cell receptor (tcr) heterodimer in complex with an anti-tcr fab fragment derived from a mitogenic antibody
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Structure:
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N15 alpha-beta t-cell receptor. Chain: a, c. Engineered: yes. N15 alpha-beta t-cell receptor. Chain: b, d. Engineered: yes. H57 fab. Chain: e, g. Engineered: yes.
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Gene: n15 t-cell receptor. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: ch0 lec 3.2.8.1. Other_details: codon in. Other_details: codon in
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Biol. unit:
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Tetramer (from
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Resolution:
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2.80Å
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R-factor:
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0.243
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R-free:
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0.309
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Authors:
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J.-H.Wang,K.Lim,A.Smolyar,M.-K.Teng,J.Sacchittini,E.L.Reinherz
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Key ref:
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J.Wang
et al.
(1998).
Atomic structure of an alphabeta T cell receptor (TCR) heterodimer in complex with an anti-TCR fab fragment derived from a mitogenic antibody.
Embo J,
17,
10-26.
PubMed id:
DOI:
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Date:
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04-Aug-97
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Release date:
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28-Jan-98
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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P01852
(TCB1_MOUSE) -
T-cell receptor beta-1 chain C region from Mus musculus
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Seq:
Struc:
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173 a.a.
239 a.a.*
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DOI no:
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Embo J
17:10-26
(1998)
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PubMed id:
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Atomic structure of an alphabeta T cell receptor (TCR) heterodimer in complex with an anti-TCR fab fragment derived from a mitogenic antibody.
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J.Wang,
K.Lim,
A.Smolyar,
M.Teng,
J.Liu,
A.G.Tse,
J.Liu,
R.E.Hussey,
Y.Chishti,
C.T.Thomson,
R.M.Sweet,
S.G.Nathenson,
H.C.Chang,
J.C.Sacchettini,
E.L.Reinherz.
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ABSTRACT
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Each T cell receptor (TCR) recognizes a peptide antigen bound to a major
histocompatibility complex (MHC) molecule via a clonotypic alphabeta
heterodimeric structure (Ti) non-covalently associated with the monomorphic CD3
signaling components. A crystal structure of an alphabeta TCR-anti-TCR Fab
complex shows an Fab fragment derived from the H57 monoclonal antibody (mAb),
interacting with the elongated FG loop of the Cbeta domain, situated beneath the
Vbeta domain. This loop, along with the partially exposed ABED beta sheet of
Cbeta, and glycans attached to both Cbeta and Calpha domains, forms a cavity of
sufficient size to accommodate a single non-glycosylated Ig domain such as the
CD3epsilon ectodomain. That this asymmetrically localized site is embedded
within the rigid constant domain module has implications for the mechanism of
signal transduction in both TCR and pre-TCR complexes. Furthermore, quaternary
structures of TCRs vary significantly even when they bind the same MHC molecule,
as manifested by a unique twisting of the V module relative to the C module.
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Selected figure(s)
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Figure 3.
Figure 3 Superposition of different TCRs defines substantial
quaternary structural variations.  -carbon
trace comparing the two N15 TCRs in the asymmetric unit (left)
as well as the N15A TCR with the 2C TCR (right). N15A (red),
N15B (white) and 2C (green) were superimposed using C  framework
residues 144 -149, 158 -161, 172 -174, 192 -197 and 212 -215.
The r.m.s. deviation for this C region is 0.19 Å between N15A
and N15B, and 0.32 Å between N15A and 2C. The side view (bottom)
shows the complete TCR
heterodimers. The top view (top) shows only the overlay of the V
modules for simplicity. The variation in quaternary structure
between N15 and 2C is quantitated in Table II.
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Figure 5.
Figure 5 N15 CDR3 residues involved in recognition of the
VSV8/Kb antigen -MHC class I complex. The figure is shown as a
GRASP (Nicholls et al., 1991) molecular surface representation,
viewing the ligand binding surface of the TCR. The V domain
is shown in blue-grey and the V domain
is shown in pink. Individual CDR3 and
residues,
whose mutation to alanine results in  1000-fold
reduction in sensitivity of T cell hybridoma transfectants to
varying molar concentrations of VSV8 peptide pulsed onto R8
antigen presenting cells, are shown in red. The CDR3 Asn101
residue which reduces recognition 100 fold is shown in yellow
and the CDR3 Glu105
residue, which has no detectable effect on recognition, is shown
in green.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Embo J
(1998,
17,
10-26)
copyright 1998.
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Figures were
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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G.I.van Boxel,
S.Holmes,
L.Fugger,
and
E.Y.Jones
(2010).
An alternative conformation of the T-cell receptor alpha constant region.
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J Mol Biol,
400,
828-837.
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PDB code:
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I.Arechaga,
M.Swamy,
D.Abia,
W.A.Schamel,
B.Alarcón,
and
J.M.Valpuesta
(2010).
Structural characterization of the TCR complex by electron microscopy.
|
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Int Immunol,
22,
897-903.
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|
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J.B.Huppa,
M.Axmann,
M.A.Mörtelmaier,
B.F.Lillemeier,
E.W.Newell,
M.Brameshuber,
L.O.Klein,
G.J.Schütz,
and
M.M.Davis
(2010).
TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity.
|
| |
Nature,
463,
963-967.
|
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|
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|
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N.Soetandyo,
Q.Wang,
Y.Ye,
and
L.Li
(2010).
Role of intramembrane charged residues in the quality control of unassembled T-cell receptor alpha-chains at the endoplasmic reticulum.
|
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J Cell Sci,
123,
1031-1038.
|
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S.Di Tommaso,
R.Antonacci,
S.Ciccarese,
and
S.Massari
(2010).
Extensive analysis of D-J-C arrangements allows the identification of different mechanisms enhancing the diversity in sheep T cell receptor beta-chain repertoire.
|
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BMC Genomics,
11,
3.
|
|
|
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S.T.Kim,
K.Takeuchi,
Z.Y.Sun,
M.Touma,
C.E.Castro,
A.Fahmy,
M.J.Lang,
G.Wagner,
and
E.L.Reinherz
(2009).
The alphabeta T cell receptor is an anisotropic mechanosensor.
|
| |
J Biol Chem,
284,
31028-31037.
|
|
|
|
|
|
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T.Beddoe,
Z.Chen,
C.S.Clements,
L.K.Ely,
S.R.Bushell,
J.P.Vivian,
L.Kjer-Nielsen,
S.S.Pang,
M.A.Dunstone,
Y.C.Liu,
W.A.Macdonald,
M.A.Perugini,
M.C.Wilce,
S.R.Burrows,
A.W.Purcell,
T.Tiganis,
S.P.Bottomley,
J.McCluskey,
and
J.Rossjohn
(2009).
Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor.
|
| |
Immunity,
30,
777-788.
|
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|
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X.Du,
J.Cheng,
and
J.Song
(2009).
Identifying protein-protein interaction sites using covering algorithm.
|
| |
Int J Mol Sci,
10,
2190-2202.
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|
|
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|
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E.J.Collins,
and
D.S.Riddle
(2008).
TCR-MHC docking orientation: natural selection, or thymic selection?
|
| |
Immunol Res,
41,
267-294.
|
|
|
|
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|
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B.Rubin,
M.Knibiehler,
and
J.E.Gairin
(2007).
Allosteric changes in the TCR/CD3 structure upon interaction with extra- or intra-cellular ligands.
|
| |
Scand J Immunol,
66,
228-237.
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|
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|
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M.S.Kuhns,
and
M.M.Davis
(2007).
Disruption of extracellular interactions impairs T cell receptor-CD3 complex stability and signaling.
|
| |
Immunity,
26,
357-369.
|
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|
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|
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R.Bello,
M.J.Feito,
G.Ojeda,
P.Portolés,
and
J.M.Rojo
(2007).
Loss of N-terminal charged residues of mouse CD3 epsilon chains generates isoforms modulating antigen T cell receptor-mediated signals and T cell receptor-CD3 interactions.
|
| |
J Biol Chem,
282,
22324-22334.
|
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|
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|
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M.A.Amon,
M.Ali,
V.Bender,
Y.N.Chan,
I.Toth,
and
N.Manolios
(2006).
Lipidation and glycosylation of a T cell antigen receptor (TCR) transmembrane hydrophobic peptide dramatically enhances in vitro and in vivo function.
|
| |
Biochim Biophys Acta,
1763,
879-888.
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|
|
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|
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M.G.Rudolph,
R.L.Stanfield,
and
I.A.Wilson
(2006).
How TCRs bind MHCs, peptides, and coreceptors.
|
| |
Annu Rev Immunol,
24,
419-466.
|
|
|
|
|
|
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S.Yamasaki,
E.Ishikawa,
M.Sakuma,
K.Ogata,
K.Sakata-Sogawa,
M.Hiroshima,
D.L.Wiest,
M.Tokunaga,
and
T.Saito
(2006).
Mechanistic basis of pre-T cell receptor-mediated autonomous signaling critical for thymocyte development.
|
| |
Nat Immunol,
7,
67-75.
|
|
|
|
|
|
|
H.Li,
S.Van Vranken,
Y.Zhao,
Z.Li,
Y.Guo,
L.Eisele,
and
Y.Li
(2005).
Crystal structures of T cell receptor (beta) chains related to rheumatoid arthritis.
|
| |
Protein Sci,
14,
3025-3038.
|
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PDB codes:
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Y.Li,
Y.Huang,
J.Lue,
J.A.Quandt,
R.Martin,
and
R.A.Mariuzza
(2005).
Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule.
|
| |
EMBO J,
24,
2968-2979.
|
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PDB code:
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|
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|
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L.Kjer-Nielsen,
M.A.Dunstone,
L.Kostenko,
L.K.Ely,
T.Beddoe,
N.A.Mifsud,
A.W.Purcell,
A.G.Brooks,
J.McCluskey,
and
J.Rossjohn
(2004).
Crystal structure of the human T cell receptor CD3 epsilon gamma heterodimer complexed to the therapeutic mAb OKT3.
|
| |
Proc Natl Acad Sci U S A,
101,
7675-7680.
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PDB code:
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M.A.Dunstone,
L.Kjer-Nielsen,
L.Kostenko,
A.W.Purcell,
A.G.Brooks,
J.Rossjohn,
and
J.McCluskey
(2004).
The production and purification of the human T-cell receptors, the CD3epsilongamma and CD3epsilondelta heterodimers: complex formation and crystallization with OKT3, a therapeutic monoclonal antibody.
|
| |
Acta Crystallogr D Biol Crystallogr,
60,
1425-1428.
|
|
|
|
|
|
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Q.Pan,
A.S.Gollapudi,
and
V.P.Dave
(2004).
Biochemical evidence for the presence of a single CD3delta and CD3gamma chain in the surface T cell receptor/CD3 complex.
|
| |
J Biol Chem,
279,
51068-51074.
|
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|
|
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|
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Z.Y.Sun,
S.T.Kim,
I.C.Kim,
A.Fahmy,
E.L.Reinherz,
and
G.Wagner
(2004).
Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.
|
| |
Proc Natl Acad Sci U S A,
101,
16867-16872.
|
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PDB code:
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|
D.Housset,
and
B.Malissen
(2003).
What do TCR-pMHC crystal structures teach us about MHC restriction and alloreactivity?
|
| |
Trends Immunol,
24,
429-437.
|
|
|
|
|
|
|
L.Kjer-Nielsen,
C.S.Clements,
A.W.Purcell,
A.G.Brooks,
J.C.Whisstock,
S.R.Burrows,
J.McCluskey,
and
J.Rossjohn
(2003).
A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity.
|
| |
Immunity,
18,
53-64.
|
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PDB code:
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|
|
R.H.McMahan,
L.Watson,
R.Meza-Romero,
G.G.Burrows,
D.N.Bourdette,
and
A.C.Buenafe
(2003).
Production, characterization, and immunogenicity of a soluble rat single chain T cell receptor specific for an encephalitogenic peptide.
|
| |
J Biol Chem,
278,
30961-30970.
|
|
|
|
|
|
|
S.Radaev,
and
P.D.Sun
(2003).
Structure and function of natural killer cell surface receptors.
|
| |
Annu Rev Biophys Biomol Struct,
32,
93.
|
|
|
|
|
|
|
Z.Wang,
and
J.Moult
(2003).
Three-dimensional structural location and molecular functional effects of missense SNPs in the T cell receptor Vbeta domain.
|
| |
Proteins,
53,
748-757.
|
|
|
|
|
|
|
C.S.Clements,
L.Kjer-Nielsen,
W.A.MacDonald,
A.G.Brooks,
A.W.Purcell,
J.McCluskey,
and
J.Rossjohn
(2002).
The production, purification and crystallization of a soluble heterodimeric form of a highly selected T-cell receptor in its unliganded and liganded state.
|
| |
Acta Crystallogr D Biol Crystallogr,
58,
2131-2134.
|
|
|
|
|
|
|
G.Werlen,
and
E.Palmer
(2002).
The T-cell receptor signalosome: a dynamic structure with expanding complexity.
|
| |
Curr Opin Immunol,
14,
299-305.
|
|
|
|
|
|
|
L.Kjer-Nielsen,
C.S.Clements,
A.G.Brooks,
A.W.Purcell,
J.McCluskey,
and
J.Rossjohn
(2002).
The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance.
|
| |
Structure,
10,
1521-1532.
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PDB code:
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M.G.Rudolph,
J.G.Luz,
and
I.A.Wilson
(2002).
Structural and thermodynamic correlates of T cell signaling.
|
| |
Annu Rev Biophys Biomol Struct,
31,
121-149.
|
|
|
|
|
|
|
T.Sasada,
M.Touma,
H.C.Chang,
L.K.Clayton,
J.H.Wang,
and
E.L.Reinherz
(2002).
Involvement of the TCR Cbeta FG loop in thymic selection and T cell function.
|
| |
J Exp Med,
195,
1419-1431.
|
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|
|
|
|
|
C.Gouaillard,
A.Huchenq-Champagne,
J.Arnaud,
C.L.Chen Cl,
and
B.Rubin
(2001).
Evolution of T cell receptor (TCR) alpha beta heterodimer assembly with the CD3 complex.
|
| |
Eur J Immunol,
31,
3798-3805.
|
|
|
|
|
|
|
K.E.Willard-Gallo,
M.Furtado,
A.Burny,
and
S.M.Wolinsky
(2001).
Down-modulation of TCR/CD3 surface complexes after HIV-1 infection is associated with differential expression of the viral regulatory genes.
|
| |
Eur J Immunol,
31,
969-979.
|
|
|
|
|
|
|
P.M.Rudd,
T.Elliott,
P.Cresswell,
I.A.Wilson,
and
R.A.Dwek
(2001).
Glycosylation and the immune system.
|
| |
Science,
291,
2370-2376.
|
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|
|
|
Z.J.Sun,
K.S.Kim,
G.Wagner,
and
E.L.Reinherz
(2001).
Mechanisms contributing to T cell receptor signaling and assembly revealed by the solution structure of an ectodomain fragment of the CD3 epsilon gamma heterodimer.
|
| |
Cell,
105,
913-923.
|
|
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PDB code:
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|
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|
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J.Foote,
and
A.Raman
(2000).
A relation between the principal axes of inertia and ligand binding.
|
| |
Proc Natl Acad Sci U S A,
97,
978-983.
|
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|
K.G.Johnson,
S.K.Bromley,
M.L.Dustin,
and
M.L.Thomas
(2000).
A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation.
|
| |
Proc Natl Acad Sci U S A,
97,
10138-10143.
|
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|
|
D.N.Garboczi,
and
W.E.Biddison
(1999).
Shapes of MHC restriction.
|
| |
Immunity,
10,
1-7.
|
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|
|
E.P.Grant,
M.Degano,
J.P.Rosat,
S.Stenger,
R.L.Modlin,
I.A.Wilson,
S.A.Porcelli,
and
M.B.Brenner
(1999).
Molecular recognition of lipid antigens by T cell receptors.
|
| |
J Exp Med,
189,
195-205.
|
|
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|
|
|
G.Fernández-Miguel,
B.Alarcón,
A.Iglesias,
H.Bluethmann,
M.Alvarez-Mon,
E.Sanz,
and
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(1999).
Multivalent structure of an alphabetaT cell receptor.
|
| |
Proc Natl Acad Sci U S A,
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|
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|
H.Li,
A.Llera,
E.L.Malchiodi,
and
R.A.Mariuzza
(1999).
The structural basis of T cell activation by superantigens.
|
| |
Annu Rev Immunol,
17,
435-466.
|
|
|
|
|
|
|
J.H.Wang,
A.Smolyar,
K.Tan,
J.H.Liu,
M.Kim,
Z.Y.Sun,
G.Wagner,
and
E.L.Reinherz
(1999).
Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors.
|
| |
Cell,
97,
791-803.
|
|
|
PDB code:
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|
|
|
|
|
K.C.Garcia,
L.Teyton,
and
I.A.Wilson
(1999).
Structural basis of T cell recognition.
|
| |
Annu Rev Immunol,
17,
369-397.
|
|
|
|
|
|
|
K.C.Garcia
(1999).
Molecular interactions between extracellular components of the T-cell receptor signaling complex.
|
| |
Immunol Rev,
172,
73-85.
|
|
|
|
|
|
|
P.S.Andersen,
P.M.Lavoie,
R.P.Sékaly,
H.Churchill,
D.M.Kranz,
P.M.Schlievert,
K.Karjalainen,
and
R.A.Mariuzza
(1999).
Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes.
|
| |
Immunity,
10,
473-483.
|
|
|
|
|
|
|
S.Degermann,
G.Sollami,
and
K.Karjalainen
(1999).
T cell receptor beta chain lacking the large solvent-exposed Cbeta FG loop supports normal alpha/beta T cell development and function in transgenic mice.
|
| |
J Exp Med,
189,
1679-1684.
|
|
|
|
|
|
|
Y.H.Ding,
B.M.Baker,
D.N.Garboczi,
W.E.Biddison,
and
D.C.Wiley
(1999).
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical.
|
| |
Immunity,
11,
45-56.
|
|
|
PDB codes:
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|
|
F.Wang,
T.Ono,
A.M.Kalergis,
W.Zhang,
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Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B.
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Immunity,
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PDB code:
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H.Li,
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PDB code:
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Y.H.Ding,
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Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids.
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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
code is
shown on the right.
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