 |
PDBsum entry 2nx5
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
2nx5
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
276 a.a.
|
|
|
|
|
|
|
|
|
|
|
99 a.a.
|
|
|
|
|
|
|
|
|
|
|
11 a.a.
|
|
|
|
|
|
|
|
|
|
|
188 a.a.
|
|
|
|
|
|
|
|
|
|
|
243 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
A t cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class i molecule.
|
|
|
Authors
|
|
F.E.Tynan,
H.H.Reid,
L.Kjer-Nielsen,
J.J.Miles,
M.C.Wilce,
L.Kostenko,
N.A.Borg,
N.A.Williamson,
T.Beddoe,
A.W.Purcell,
S.R.Burrows,
J.Mccluskey,
J.Rossjohn.
|
|
|
Ref.
|
|
Nat Immunol, 2007,
8,
268-276.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Plasticity of the T cell receptor (TCR) is a hallmark of major
histocompatibility complex (MHC)-restricted T cell recognition. However, it is
unclear whether interactions of TCR and peptide-MHC class I (pMHCI) always
conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its
non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr
virus peptide bound to HLA-B(*)3501. This complex was atypical of previously
characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled
the bulged antigenic determinant. This peptide 'bulldozing' created a more
featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts
essential for MHC class I restriction of TCR recognition. Our findings represent
a mechanism of antigen recognition whereby the plasticity of the T cell response
is dictated mainly by adjustments in the MHC-bound peptide.
|
|
|
|
|
|
|
|
Figure 2.
(a) ELS4 TCR 'footprint'. Surface representation of
HLA-B^*3501 'looking down' into the peptide-binding cleft.
HLA-B^*3501, gray; EPLP peptide, dark gray; colors of pMHCI
residues that contact the TCR are according to that of the
relevant contacting CDR loop (as described in Fig. 1), and
peptide residues are identified in red by one-letter amino-acid
designation followed by position number. (b) SB27 TCR
'footprint'. Surface representation of HLA-B^*3508 'looking
down' into the peptide-binding cleft. HLA-B^*3508, gray; LPEP
peptide, dark gray; other colors as described in a.
|
|
Figure 4.
(a) The ELS4 TCR crumples the EPLP peptide. Non-ligand-bound
(yellow) and ligand-bound (orange) conformation of the EPLP
peptide. ELS4 V  domain,
magenta; ELS4 V[  ]domain,
cyan. 1
and 2
helices of ligand-bound HLA-B^*3501, gray ribbon. For clarity,
the peptide is presented without the backbone details and
includes only the side chains. (b,c) Peptide conformational
changes with distinct views. Non-ligand-bound (yellow with black
labels) and ligand-bound (orange with red labels) conformation
of the EPLP peptide. HLA-B^*3501 1
and 2
helices, gray ribbon. The 2
helix is removed from b for clarity. (d) Peptide interactions
with the ELS4 TCR.
|
|
|
|
|
|
The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Immunol
(2007,
8,
268-276)
copyright 2007.
|
|
|
|
|
|
|
