ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structural arrangement of the transmission interface in the antigen ABC transport complex TAP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A comprehensive family-based replication study of schizophrenia genes.JAMA psychiatry · 2013Pooled it
- Bidirectional communication between nucleotide and substrate binding sites in a type IV multidrug ABC transporter.Nature communications · 2025Article
- Interdomain communication in a homodimeric ABC transporter.The Journal of biological chemistry · 2024Article
- Probing the allosteric NBD-TMD crosstalk in the ABC transporter MsbA by solid-state NMR.Communications biology · 2024Article
- IntracellularFrontiers in immunology · 2023Article
- The Lack of STING Impairs the MHC-I Dependent Antigen Presentation and JAK/STAT Signaling in Murine Macrophages.International journal of molecular sciences · 2022Article
- Pharmacological disruption of the MTDH-SND1 complex enhances tumor antigen presentation and synergizes with anti-PD-1 therapy in metastatic breast cancer.Nature cancer · 2022Article
- A Conserved Motif in Intracellular Loop 1 Stabilizes the Outward-Facing Conformation of TmrAB.Journal of molecular biology · 2021Article
- The first intracellular loop is essential for the catalytic cycle of the human ABCG2 multidrug resistance transporter.FEBS letters · 2020Article
- Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA fromCommunications biology · 2019Article
- Midgut transcriptomal response of the rice leaffolder, Cnaphalocrocis medinalis (Guenée) to Cry1C toxin.PloS one · 2018Article
- The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling.Frontiers in immunology · 2018Review
- 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
- Article
- Plausible Drug Targets in the Streptococcus mutans Quorum Sensing Pathways to Combat Dental Biofilms and Associated Risks.Indian journal of microbiology · 2015Review
- Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch.Scientific reports · 2015Article
- Use of Functional Polymorphisms To Elucidate the Peptide Binding Site of TAP Complexes.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): CLOSED AND OPEN STATE CHANNEL MODELS.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transporter associated with antigen processing (TAP) represents a focal point in the immune recognition of virally or malignantly transformed cells by translocating proteasomal degradation products into the endoplasmic reticulum-lumen for loading of MHC class I molecules. Based on a number of experimental data and the homology to the bacterial ABC exporter Sav1866, we constructed a 3D structural model of the core TAP complex and used it to examine the interface between the transmembrane and nucleotide-binding domains (NBD) by cysteine-scanning and cross-linking approaches. Herein, we demonstrate the functional importance of the newly identified X-loop in the NBD in coupling substrate binding to downstream events in the transport cycle. We further verified domain swapping in a heterodimeric ABC half-transporter complex by cysteine cross-linking. Strikingly, either substrate binding or translocation can be blocked by cross-linking the X-loop to coupling helix 2 or 1, respectively. These results resolve the structural arrangement of the transmission interface and point to different functions of the cytosolic loops and coupling helices in substrate binding, signaling, and transport.
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