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PDBsum entry 3f8u
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Immune system/isomerase
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PDB id
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3f8u
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References listed in PDB file
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Key reference
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Title
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Insights into mhc class i peptide loading from the structure of the tapasin-Erp57 thiol oxidoreductase heterodimer.
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Authors
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G.Dong,
P.A.Wearsch,
D.R.Peaper,
P.Cresswell,
K.M.Reinisch.
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Ref.
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Immunity, 2009,
30,
21-32.
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PubMed id
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Abstract
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Tapasin is a glycoprotein critical for loading major histocompatibility complex
(MHC) class I molecules with high-affinity peptides. It functions within the
multimeric peptide-loading complex (PLC) as a disulfide-linked, stable
heterodimer with the thiol oxidoreductase ERp57, and this covalent interaction
is required to support optimal PLC activity. Here, we present the 2.6 A
resolution structure of the tapasin-ERp57 core of the PLC. The structure
revealed that tapasin interacts with both ERp57 catalytic domains, accounting
for the stability of the heterodimer, and provided an example of a protein
disulfide isomerase family member interacting with substrate. Mutational
analysis identified a conserved surface on tapasin that interacted with MHC
class I molecules and was critical for peptide loading and editing functions of
the tapasin-ERp57 heterodimer. By combining the tapasin-ERp57 structure with
those of other defined PLC components, we present a molecular model that
illuminates the processes involved in MHC class I peptide loading.
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