 |
PDBsum entry 3kpp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
3kpp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
T cell allorecognition via molecular mimicry.
|
|
|
Authors
|
|
W.A.Macdonald,
Z.Chen,
S.Gras,
J.K.Archbold,
F.E.Tynan,
C.S.Clements,
M.Bharadwaj,
L.Kjer-Nielsen,
P.M.Saunders,
M.C.Wilce,
F.Crawford,
B.Stadinsky,
D.Jackson,
A.G.Brooks,
A.W.Purcell,
J.W.Kappler,
S.R.Burrows,
J.Rossjohn,
J.Mccluskey.
|
|
|
Ref.
|
|
Immunity, 2009,
31,
897-908.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
T cells often alloreact with foreign human leukocyte antigens (HLA). Here we
showed the LC13 T cell receptor (TCR), selected for recognition on self-HLA-B(
*)0801 bound to a viral peptide, alloreacts with B44 allotypes (HLA-B( *)4402
and HLA-B( *)4405) bound to two different allopeptides. Despite extensive
polymorphism between HLA-B( *)0801, HLA-B( *)4402, and HLA-B( *)4405 and the
disparate sequences of the viral and allopeptides, the LC13 TCR engaged these
peptide-HLA (pHLA) complexes identically, accommodating mimicry of the viral
peptide by the allopeptide. The viral and allopeptides adopted similar
conformations only after TCR ligation, revealing an induced-fit mechanism of
molecular mimicry. The LC13 T cells did not alloreact against HLA-B( *)4403, and
the single residue polymorphism between HLA-B( *)4402 and HLA-B( *)4403 affected
the plasticity of the allopeptide, revealing that molecular mimicry was
associated with TCR specificity. Accordingly, molecular mimicry that is HLA and
peptide dependent is a mechanism for human T cell alloreactivity between
disparate cognate and allogeneic pHLA complexes.
|
|
|
|
|
|
|
