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PDBsum entry 2bsv
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Immune system
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PDB id
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2bsv
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References listed in PDB file
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Key reference
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Title
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T cell cross-Reactivity and conformational changes during tcr engagement.
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Authors
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J.K.Lee,
G.Stewart-Jones,
T.Dong,
K.Harlos,
K.Di gleria,
L.Dorrell,
D.C.Douek,
P.A.Van der merwe,
E.Y.Jones,
A.J.Mcmichael.
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Ref.
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J Exp Med, 2004,
200,
1455-1466.
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PubMed id
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Abstract
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All thymically selected T cells are inherently cross-reactive, yet many data
indicate a fine specificity in antigen recognition, which enables virus escape
from immune control by mutation in infections such as the human immunodeficiency
virus (HIV). To address this paradox, we analyzed the fine specificity of T
cells recognizing a human histocompatibility leukocyte antigen
(HLA)-A2-restricted, strongly immunodominant, HIV gag epitope (SLFNTVATL). The
majority of 171 variant peptides tested bound HLA-A2, but only one third were
recognized. Surprisingly, one recognized variant (SLYNTVATL) showed marked
differences in structure when bound to HLA-A2. T cell receptor (TCR) recognition
of variants of these two peptides implied that they adopted the same
conformation in the TCR-peptide-major histocompatibility complex (MHC) complex.
However, the on-rate kinetics of TCR binding were identical, implying that
conformational changes at the TCR-peptide-MHC binding interface occur after an
initial permissive antigen contact. These findings have implications for the
rational design of vaccines targeting viruses with unstable genomes.
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