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Figure 4.
Figure 4. SB27 TCR recognition of the HLA-B^*3508-LPEP complex
is antibody like and is dominated by TCR-peptide interactions.
(a,b) GRASP image of the SB27 TCR-peptide interaction (a)
compared with that of a complex between an Fab and a peptide
from human rhinovirus viral capsid protein VP2 (b; Protein Data
Bank accession number, 1A3R)46. TCR V[ ]and
Fab V[H], red; TCR V and
Fab V[L], blue; Epstein-Barr virus LPEP and rhinovirus VP2
peptides, yellow. (c) Closer view of the SB27 TCR interactions
with the solvent-exposed side chains of the LPEP peptide.
Peptide, orange; CDR loop colors are as in Figure 1b. (d)
Dose-response assays of analogs of the 13-residue peptide
(LPEPLPQGQLTAY) that include single-amino acid substitutions,
assessing recognition by SB27 CTLs (chromium-release assays,
left) and binding to 'empty' HLA-B^*3508 with the transporter
associated with antigen processing-deficient T2-B^*3508 (right).
Peptides recognized well in the cytotoxicity assays are assumed
to bind well to HLA-B^*3508 and are therefore excluded from the
MHC-binding assays (NT). Data represent peptide concentrations
for half-maximal lysis or binding calculated from dose-response
curves for each peptide and are representative of two
independent experiments with similar results.
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