ArticleJournal of immunology (Baltimore, Md. : 1950)2015
Use of Functional Polymorphisms To Elucidate the Peptide Binding Site of TAP Complexes.
Article in Journal of immunology (Baltimore, Md. : 1950), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- Principles of peptide selection by the transporter associated with antigen processing.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The lysosomal transporter TAPL has a dual role as peptide translocator and phosphatidylserine floppase.Nature communications · 2022Article
- Spotlight on TAP and its vital role in antigen presentation and cross-presentation.Molecular immunology · 2022Review
- New vistas unfold: Chicken MHC molecules reveal unexpected ways to present peptides to the immune system.Frontiers in immunology · 2022Review
- Selecting for Altered Substrate Specificity Reveals the Evolutionary Flexibility of ATP-Binding Cassette Transporters.Current biology : CB · 2020Article
- Mechanics and pharmacology of substrate selection and transport by eukaryotic ABC exporters.Nature structural & molecular biology · 2019Review
- Moving the Cellular Peptidome by Transporters.Frontiers in cell and developmental biology · 2018Review
- A highly conserved sequence of the viral TAP inhibitor ICP47 is required for freezing of the peptide transport cycle.Scientific reports · 2017Article
- Structure and Dynamics of Antigenic Peptides in Complex with TAP.Frontiers in immunology · 2017Review
- Structure of the transporter associated with antigen processing trapped by herpes simplex virus.eLife · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
TAP1/TAP2 complexes translocate peptides from the cytosol to the endoplasmic reticulum lumen to enable immune surveillance by CD8(+) T cells. Peptide transport is preceded by peptide binding to a cytosol-accessible surface of TAP1/TAP2 complexes, but the location of the TAP peptide-binding pocket remains unknown. Guided by the known contributions of polymorphic TAP variants to peptide selection, we combined homology modeling of TAP with experimental measurements to identify several TAP residues that interact with peptides. Models for peptide-TAP complexes were generated, which indicate bent conformation for peptides. The peptide binding site of TAP is located at the hydrophobic boundary of the cytosolic membrane leaflet, with striking parallels to the glutathione binding site of NaAtm1, a transporter that functions in bacterial heavy metal detoxification. These studies illustrate the conservation of the ligand recognition modes of bacterial and mammalians transporters involved in peptide-guided cellular surveillance.
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Registered trials
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