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Literature summary for 7.4.2.14 extracted from

  • Blees, A.; Januliene, D.; Hofmann, T.; Koller, N.; Schmidt, C.; Trowitzsch, S.; Moeller, A.; Tampe, R.
    Structure of the human MHC-I peptide-loading complex (2017), Nature, 551, 525-528 .
    View publication on PubMed
Search for more literature for 7.4.2.14

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane
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 Homo sapiens 5789
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q03518 AND Q03519 TAP1 and TAP2 subunits
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Source Tissue

Source Tissue Comment Organism Textmining
Burkitt lymphoma cell
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 Homo sapiens
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Synonyms

Synonyms Comment Organism
TAP
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 Homo sapiens
TAP1
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 Homo sapiens
TAP2
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 Homo sapiens
transporter associated with antigen processing
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 Homo sapiens

General Information

General Information Comment Organism
metabolism the peptide-loading complex (PLC) is a transient, multisubunit membrane complex in the endoplasmic reticulum that is essential for establishing a hierarchical immune response. The PLC coordinates peptide translocation into the endoplasmic reticulum with loading and editing of major histocompatibility complex class I (MHC-I) molecules. After final proofreading in the PLC, stable peptide-MHC-I complexes are released to the cell surface to evoke a T-cell response against infected or malignant cells. Sampling of different MHC-I allomorphs requires the precise coordination of seven different subunits in a single macromolecular assembly, including the transporter associated with antigen processing (TAP1 and TAP2, jointly referred to as TAP), the oxidoreductase ERp57, the MHC-I heterodimer, and the chaperones tapasin and calreticulin. Molecular organization of and mechanistic events taking place in the PLC. Two endoplasmic reticulum-resident editing modules composed of tapasin, calreticulin, ERp57, and MHC-I are centred around TAP in a pseudo-symmetric orientation. A multivalent chaperone network within and across the editing modules establishes the proofreading function at two lateral binding platforms for MHC-I molecules Homo sapiens
additional information isolation of human PLC from Burkitt's lymphoma cells using an engineered viral inhibitor as bait and determination of the structure of native PLC by electron cryo-microscopy, overview Homo sapiens