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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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8 terms
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Biological process
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immune response
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8 terms
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Biochemical function
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protein binding
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1 term
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DOI no:
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J Exp Med
189:359-370
(1999)
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PubMed id:
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Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry.
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R.Zhao,
D.J.Loftus,
E.Appella,
E.J.Collins.
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ABSTRACT
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The T cell receptor (TCR), from a xeno-reactive murine cytotoxic T lymphocyte
clone AHIII12.2, recognizes murine H-2Db complexed with peptide p1027
(FAPGVFPYM), as well as human HLA-A2.1 complexed with peptide p1049 (ALWGFFPVL).
A commonly proposed model (the molecular mimicry model) used to explain TCR
cross-reactivity suggests that the molecular surfaces of the recognized
complexes are similar in shape, charge, or both, in spite of the primary
sequence differences. To examine the mechanism of xeno-reactivity of AHIII12.2,
we have determined the crystal structures of A2/p1049 and Db/p1027 to 2.5 A and
2.8 A resolution, respectively. The crystal structures show that the TCR
footprint regions of the two class I complexes are significantly different in
shape and charge. We propose that rather than simple molecular mimicry,
unpredictable arrays of common and differential contacts on the two class I
complexes are used for their recognition by the same TCR.
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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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A.Theodossis,
C.Guillonneau,
A.Welland,
L.K.Ely,
C.S.Clements,
N.A.Williamson,
A.I.Webb,
J.A.Wilce,
R.J.Mulder,
M.A.Dunstone,
P.C.Doherty,
J.McCluskey,
A.W.Purcell,
S.J.Turner,
and
J.Rossjohn
(2010).
Constraints within major histocompatibility complex class I restricted peptides: presentation and consequences for T-cell recognition.
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Proc Natl Acad Sci U S A, 107,
5534-5539.
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D.A.Antunes,
G.F.Vieira,
M.M.Rigo,
S.P.Cibulski,
M.Sinigaglia,
and
J.A.Chies
(2010).
Structural allele-specific patterns adopted by epitopes in the MHC-I cleft and reconstruction of MHC:peptide complexes to cross-reactivity assessment.
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PLoS One, 5,
e10353.
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E.F.Young,
P.R.Hess,
L.W.Arnold,
R.Tisch,
and
J.A.Frelinger
(2009).
Islet lymphocyte subsets in male and female NOD mice are qualitatively similar but quantitatively distinct.
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Autoimmunity, 42,
678-691.
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P.Kumar,
A.Vahedi-Faridi,
W.Saenger,
A.Ziegler,
and
B.Uchanska-Ziegler
(2009).
Conformational changes within the HLA-A1:MAGE-A1 complex induced by binding of a recombinant antibody fragment with TCR-like specificity.
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Protein Sci, 18,
37-49.
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PDB code:
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M.T.Greene,
A.M.Ercolini,
M.DeGutes,
and
S.D.Miller
(2008).
Differential induction of experimental autoimmune encephalomyelitis by myelin basic protein molecular mimics in mice humanized for HLA-DR2 and an MBP(85-99)-specific T cell receptor.
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J Autoimmun, 31,
399-407.
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A.N.Khitrov,
Z.S.Shogenov,
E.B.Tretyak,
A.I.Ischenko,
E.Matsuura,
O.Neuhaus,
M.A.Paltsev,
and
S.V.Suchkov
(2007).
Postinfectious immunodeficiency and autoimmunity: pathogenic and clinical values and implications.
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Expert Rev Clin Immunol, 3,
323-331.
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A.J.Bordner,
and
R.Abagyan
(2006).
Ab initio prediction of peptide-MHC binding geometry for diverse class I MHC allotypes.
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Proteins, 63,
512-526.
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H.H.Bui,
A.J.Schiewe,
H.von Grafenstein,
and
I.S.Haworth
(2006).
Structural prediction of peptides binding to MHC class I molecules.
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Proteins, 63,
43-52.
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O.Y.Borbulevych,
T.K.Baxter,
Z.Yu,
N.P.Restifo,
and
B.M.Baker
(2005).
Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design.
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J Immunol, 174,
4812-4820.
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PDB codes:
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P.S.Rohrlich,
N.Fazilleau,
F.Ginhoux,
H.Firat,
F.Michel,
M.Cochet,
N.Laham,
M.P.Roth,
S.Pascolo,
F.Nato,
H.Coppin,
P.Charneau,
O.Danos,
O.Acuto,
R.Ehrlich,
J.Kanellopoulos,
and
F.A.Lemonnier
(2005).
Direct recognition by alphabeta cytolytic T cells of Hfe, a MHC class Ib molecule without antigen-presenting function.
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Proc Natl Acad Sci U S A, 102,
12855-12860.
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R.Olson,
K.E.Huey-Tubman,
C.Dulac,
and
P.J.Bjorkman
(2005).
Structure of a pheromone receptor-associated MHC molecule with an open and empty groove.
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PLoS Biol, 3,
e257.
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PDB code:
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A.P.Kohm,
K.G.Fuller,
and
S.D.Miller
(2003).
Mimicking the way to autoimmunity: an evolving theory of sequence and structural homology.
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Trends Microbiol, 11,
101-105.
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J.Buslepp,
H.Wang,
W.E.Biddison,
E.Appella,
and
E.J.Collins
(2003).
A correlation between TCR Valpha docking on MHC and CD8 dependence: implications for T cell selection.
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Immunity, 19,
595-606.
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PDB code:
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P.E.Adrian,
G.Rajaseger,
V.S.Mathura,
M.K.Sakharkar,
and
P.Kangueane
(2002).
Types of inter-atomic interactions at the MHC-peptide interface: identifying commonality from accumulated data.
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BMC Struct Biol, 2,
2.
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M.H.Heemskerk,
R.A.de Paus,
E.G.Lurvink,
F.Koning,
A.Mulder,
R.Willemze,
J.J.van Rood,
and
J.H.Falkenburg
(2001).
Dual HLA class I and class II restricted recognition of alloreactive T lymphocytes mediated by a single T cell receptor complex.
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Proc Natl Acad Sci U S A, 98,
6806-6811.
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A.Simon,
Z.Dosztányi,
E.Rajnavölgyi,
and
I.Simon
(2000).
Function-related regulation of the stability of MHC proteins.
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Biophys J, 79,
2305-2313.
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M.A.Batalia,
T.J.Kirksey,
A.Sharma,
L.Jiang,
J.P.Abastado,
S.Yan,
R.Zhao,
and
E.J.Collins
(2000).
Class I MHC is stabilized against thermal denaturation by physiological concentrations of NaCl.
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Biochemistry, 39,
9030-9038.
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N.A.Watkins,
C.Brown,
C.Hurd,
C.Navarrete,
and
W.H.Ouwehand
(2000).
The isolation and characterisation of human monoclonal HLA-A2 antibodies from an immune V gene phage display library.
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Tissue Antigens, 55,
219-228.
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N.J.Felix,
W.J.Brickey,
R.Griffiths,
J.Zhang,
L.Van Kaer,
T.Coffman,
and
J.P.Ting
(2000).
H2-DMalpha(-/-) mice show the importance of major histocompatibility complex-bound peptide in cardiac allograft rejection.
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J Exp Med, 192,
31-40.
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O.Schueler-Furman,
Y.Altuvia,
A.Sette,
and
H.Margalit
(2000).
Structure-based prediction of binding peptides to MHC class I molecules: application to a broad range of MHC alleles.
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Protein Sci, 9,
1838-1846.
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R.Obst,
N.Netuschil,
K.Klopfer,
S.Stevanović,
and
H.G.Rammensee
(2000).
The role of peptides in T cell alloreactivity is determined by self-major histocompatibility complex molecules.
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J Exp Med, 191,
805-812.
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H.Auchincloss
(1999).
Literature update 1999, part 1.
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Xenotransplantation, 6,
220-223.
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K.C.Garcia
(1999).
Molecular interactions between extracellular components of the T-cell receptor signaling complex.
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Immunol Rev, 172,
73-85.
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K.Maenaka,
and
E.Y.Jones
(1999).
MHC superfamily structure and the immune system.
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Curr Opin Struct Biol, 9,
745-753.
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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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