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Structure and dynamics of antigenic peptides in complex with TAP

  • The transporter associated with antigen processing (TAP) selectively translocates antigenic peptides into the endoplasmic reticulum. Loading onto major histocompatibility complex class I molecules and proofreading of these bound epitopes are orchestrated within the macromolecular peptide-loading complex, which assembles on TAP. This heterodimeric ABC-binding cassette (ABC) transport complex is therefore a major component in the adaptive immune response against virally or malignantly transformed cells. Its pivotal role predestines TAP as a target for infectious diseases and malignant disorders. The development of therapies or drugs therefore requires a detailed comprehension of structure and function of this ABC transporter, but our knowledge about various aspects is still insufficient. This review highlights recent achievements on the structure and dynamics of antigenic peptides in complex with TAP. Understanding the binding mode of antigenic peptides in the TAP complex will crucially impact rational design of inhibitors, drug development, or vaccination strategies.

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Author:Elisa Lehnert, Robert TampéORCiDGND
URN:urn:nbn:de:hebis:30:3-451682
DOI:https://doi.org/10.3389/fimmu.2017.00010
ISSN:1664-3224
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/28194151
Parent Title (English):Frontiers in immunology
Publisher:Frontiers Research Foundation
Place of publication:Lausanne
Contributor(s):Tim Elliott
Document Type:Article
Language:English
Year of Completion:2017
Date of first Publication:2017/01/30
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2017/12/05
Tag:ABC transporter; antigen processing; ligand binding; membrane proteins; peptide-loading complex; substrate-binding site
Volume:8
Issue:Art. 10
Page Number:8
First Page:1
Last Page:8
Note:
Copyright © 2017 Lehnert and Tampé. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
HeBIS-PPN:42529465X
Institutes:Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Biowissenschaften / Biowissenschaften
Wissenschaftliche Zentren und koordinierte Programme / Center for Membrane Proteomics (CMP)
Wissenschaftliche Zentren und koordinierte Programme / Sonderforschungsbereiche / Forschungskollegs
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Open-Access-Publikationsfonds:Biowissenschaften
Licence (German):License LogoCreative Commons - Namensnennung 4.0