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PDBsum entry 1jtr
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Immune system
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PDB id
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1jtr
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Contents |
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202 a.a.
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237 a.a.
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274 a.a.
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99 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural comparison of allogeneic and syngeneic t cell receptor-Peptide-Major histocompatibility complex complexes: a buried alloreactive mutation subtly alters peptide presentation substantially increasing v(beta) interactions.
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Authors
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J.G.Luz,
M.Huang,
K.C.Garcia,
M.G.Rudolph,
V.Apostolopoulos,
L.Teyton,
I.A.Wilson.
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Ref.
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J Exp Med, 2002,
195,
1175-1186.
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PubMed id
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Abstract
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The crystal structures of the 2C/H-2K(bm3)-dEV8 allogeneic complex at 2.4 A and
H-2K(bm3)-dEV8 at 2.15 A, when compared with their syngeneic counterparts,
elucidate structural changes that induce an alloresponse. The Asp77Ser mutation
that imbues H-2K(bm3)-dEV8 with its alloreactive properties is located beneath
the peptide and does not directly contact the T cell receptor (TCR). However,
the buried mutation induces local rearrangement of the peptide itself to
preserve hydrogen bonding interactions between the peptide and the alpha(1) 77
residue. The COOH terminus of the peptide main chain is tugged toward the
alpha(1)-helix such that its presentation to the TCR is altered. These changes
increase the stability of the allogeneic peptide-major histocompatibility
complex (pMHC) complex and increase complementarity in the TCR-pMHC interface,
placing greater emphasis on recognition of the pMHC by the TCR beta-chain,
evinced by an increase in shape complementarity, buried surface area, and number
of TCR-pMHC contacting residues. A nearly fourfold increase in the number of
beta-chain-pMHC contacts is accompanied by a concomitant 64% increase in
beta-chain-pMHC shape complementarity. Thus, the allogeneic mutation causes the
same peptide to be presented differently, temporally and spatially, by the
allogeneic and syngeneic MHCs.
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