Ligand Selection and Trafficking for MHC I

Hateren, Andy van; Elliott, Tim

doi:10.1016/b978-0-12-374279-7.06008-2

Cited by 2 publications

(1 citation statement)

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“…Beginning with the determination of the structure of the chaperone tapasin bound to another stabilizing component ERp57 (also known as PDIA3) (Dong et al, 2009), several additional structures determined by X-ray crystallography (Jiang et al, 2017;Thomas & Tampe ´, 2017;Mu ¨ller et al, 2022;Jiang et al, 2022) or cryoEM (Blees et al, 2017;Domnick et al, 2022) have augmented a structure-based mechanistic view of chaperone function. Several recent review papers on this topic are primarily based on a biological perspective (Margulies et al, 2022;Margulies, Jiang et al, 2023;Turner et al, 2023;van Hateren & Elliott, 2023;Lan et al, 2023;Satti et al, 2023). This review will emphasize a structural point of view (Table 1) and the principles governing peptide exchange.…”

Section: Introductionmentioning

confidence: 99%

Chaperone-mediated MHC-I peptide exchange in antigen presentation

Jiang,

Natarajan,

Margulies

2024

IUCrJ

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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.

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