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PDBsum entry 2cii
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Immune system/peptide
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PDB id
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2cii
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References listed in PDB file
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Key reference
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Title
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The crystal structure of h-2d(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class i assembly intermediate.
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Authors
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A.Glithero,
J.Tormo,
K.Doering,
M.Kojima,
E.Y.Jones,
T.Elliott.
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Ref.
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J Biol Chem, 2006,
281,
12699-12704.
[DOI no: ]
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PubMed id
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Abstract
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In the absence of bound peptide ligands, major histocompatibility complex (MHC)
class I molecules are unstable. In an attempt to determine the minimum
requirement for peptide-dependent MHC class I stabilization, we have used short
synthetic peptides derived from the Sendai virus nucleoprotein epitope (residues
324-332, 1FAPGNYPAL9) to promote its folding in vitro of H-2D(b). We found that
H-2D(b) can be stabilized by the pentapeptide 5NYPAL9, which is equivalent to
the C-terminal portion of the optimal nonapeptide and includes both the P5 and
P9 anchor residues. We have crystallized the complex of the H-2D(b) molecule
with the pentamer and determined the structure to show how a quasi-stable MHC
class I molecule can be formed by occupancy of a single binding pocket in the
peptide-binding groove.
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Figure 1.
FIGURE 1. Dose-dependent recovery of H-2D^b molecules from
refolding reactions containing increasing concentrations of
FAPGNYPAL (  ), FAPGN (  ), NYPAL
(  ), or TYQRTRALV (x).
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Figure 4.
FIGURE 4. Comparison of peptide conformations in H-2D^b
complexes. The structure of NYPAL (green) is shown superposed
with the previously reported structures of WT (FAPGNYPAL; blue)
and K2G (FAPGS(O-GlcNAc) YPAL; red). For clarity the
Ser^5-linked glycan is omitted from the K2G structure.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
12699-12704)
copyright 2006.
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