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Chaperone-mediated MHC-I peptide exchange in antigen presentation

Authors :
Jiansheng Jiang
Kannan Natarajan
David H. Margulies
Source :
IUCrJ, Vol 11, Iss 3, Pp 287-298 (2024)
Publication Year :
2024
Publisher :
International Union of Crystallography, 2024.

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.

Details

Language :
English
ISSN :
20522525
Volume :
11
Issue :
3
Database :
Directory of Open Access Journals
Journal :
IUCrJ
Publication Type :
Academic Journal
Accession number :
edsdoj.49383e4974d0ba938c62a7c7b70d2
Document Type :
article
Full Text :
https://doi.org/10.1107/S2052252524002768