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PDBsum entry 2bck
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Immune system
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PDB id
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2bck
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References listed in PDB file
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Key reference
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Title
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Crystal structure of hla-A2402 Complexed with a telomerase peptide.
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Authors
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D.K.Cole,
P.J.Rizkallah,
F.Gao,
N.I.Watson,
J.M.Boulter,
J.I.Bell,
M.Sami,
G.F.Gao,
B.K.Jakobsen.
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Ref.
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Eur J Immunol, 2006,
36,
170-179.
[DOI no: ]
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PubMed id
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Abstract
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HLA-A*2402 is the most commonly expressed HLA allele in oriental populations. It
is also widely expressed in the Caucasian population, making it one of, if not
the most abundant HLA I types. In order to study its structure in terms of
overall fold and peptide presentation, a soluble form of this HLA I (alpha1,
alpha2, alpha3 and beta(2)m domains) has been expressed, refolded and
crystallized in complex with a cancer-related telomerase peptide (VYGFVRACL),
and its structure has been solved to 2.8 A resolution. The overall structure of
HLA-A*2402 is virtually identical to other reported peptide-HLA I structures.
However, there are distinct features observable from this structure at the HLA I
peptide binding pockets. The size and depth of pocket B makes it highly suitable
for binding to large aromatic side chains, which explains the high prevalence of
tyrosine at peptide position 2. Also, for HLA binding at peptide position 5,
there is an additional anchor point, which allows the proximal amino acids to
protrude out, providing a prominent feature for TCR interaction. Finally, pocket
F allows the anchor residue at position 9 to be bound unusually deeply within
the HLA structure.
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