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Chaperone-mediated MHC-I peptide exchange in antigen presentation.
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- Additional Information
- Source:
Publisher: International Union of Crystallography Country of Publication: England NLM ID: 101623101 Publication Model: Electronic Cited Medium: Internet ISSN: 2052-2525 (Electronic) Linking ISSN: 20522525 NLM ISO Abbreviation: IUCrJ Subsets: MEDLINE
- Publication Information:
Original Publication: Chester : International Union of Crystallography, [2014]-
- Subject Terms:
- Abstract:
This work focuses on molecules that are encoded by the major histocompatibility complex (MHC) and that bind self-, foreign- or tumor-derived peptides and display these at the cell surface for recognition by receptors on T lymphocytes (T cell receptors, TCR) and natural killer (NK) cells. The past few decades have accumulated a vast knowledge base of the structures of MHC molecules and the complexes of MHC/TCR with specificity for many different peptides. In recent years, the structures of MHC-I molecules complexed with chaperones that assist in peptide loading have been revealed by X-ray crystallography and cryogenic electron microscopy. These structures have been further studied using mutagenesis, molecular dynamics and NMR approaches. This review summarizes the current structures and dynamic principles that govern peptide exchange as these relate to the process of antigen presentation.
(open access.)
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- Contributed Indexing:
Keywords: MHC; MHC-I/TAPBPR; MHC-I/tapasin; PLC; antigen presentation; chaperones; major histocompatibility complex; peptide exchange; structural immunology
- Accession Number:
0 (Histocompatibility Antigens Class I)
0 (Molecular Chaperones)
0 (Peptides)
0 (Receptors, Antigen, T-Cell)
- Publication Date:
Date Created: 20240424 Date Completed: 20240503 Latest Revision: 20240531
- Publication Date:
20240531
- Accession Number:
PMC11067752
- Accession Number:
10.1107/S2052252524002768
- Accession Number:
38656309
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