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PDBsum entry 1nfd
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Complex (immunoreceptor/immunoglobulin)
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PDB id
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1nfd
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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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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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Ref.
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Embo J, 1998,
17,
10-26.
[DOI no: ]
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PubMed id
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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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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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Secondary reference #1
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Title
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Crystallization of a deglycosylated t cell receptor (tcr) complexed with an anti-Tcr FAB fragment.
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Authors
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J.Liu,
A.G.Tse,
H.C.Chang,
J.H.Liu,
J.Wang,
R.E.Hussey,
Y.Chishti,
B.Rheinhold,
R.Spoerl,
S.G.Nathenson,
J.C.Sacchettini,
E.L.Reinherz.
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Ref.
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J Biol Chem, 1996,
271,
33639-33646.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. Electrospray mass spectrometry analysis of
sTCR-derived glycans. A, electrospray mass spectrometry of
glycans liberated^ from the N15 sTCR by endo-H; B, collision
spectra and the deduced^ unique linkage, sequence, and branching
of the GlcNAc[2]-Man[5] glycan.
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Figure 5.
Fig. 5. Native IEF gel of sTCR derivatives. N15 TCR and
derivative proteins were compared on an IEF Phastgel (pH 3-9),
and^ the IEF gel was stained with a silver stain kit. The
calibration kit markers (pH 3-10) are indicated as pI standards
(pI Stds.). N15, N15^s, unpurified N15^s  , and
Superdex 75-purified N15^s are shown.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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