ArticleiScience2020
The Mechanism of β2m Molecule-Induced Changes in the Peptide Presentation Profile in a Bony Fish.
Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Identification and profiling of HLA-A*02:01-restrictedVirulence · 2026Article
- Design of solubly expressed miniaturized SMART MHCs.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome-Wide Identification ofMarine drugs · 2023Article
- Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular Characterization of MHC Class I Alpha 1 and 2 Domains in Asian Seabass (International journal of molecular sciences · 2022Article
- Peptide-dependent tuning of major histocompatibility complex motional properties and the consequences for cellular immunity.Current opinion in immunology · 2022Review
- The Structure of a Peptide-Loaded Shark MHC Class I Molecule Reveals Features of the Binding between βJournal of immunology (Baltimore, Md. : 1950) · 2021Article
- The Crystal Structure of the MHC Class I (MHC-I) Molecule in the Green Anole Lizard Demonstrates the Unique MHC-I System in Reptiles.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Structural Comparison Between MHC Classes I and II; in Evolution, a Class-II-Like Molecule Probably Came First.Frontiers in immunology · 2021Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Contemporary antigen presentation knowledge is based on the existence of a single β2m locus, and a classical MHC class I forms a complex with a peptide (i.e., pMHC-I) to trigger CTL immunity. However, two β2m loci have been found in diploid bony fish; the function of the two β2m molecules is unclear. Here, we determined the variant peptide profiles originating from different products of the β2m loci binding to the same MHC-I molecule and further solved the crystal structures of the two pMHC-I molecules (i.e., pCtid-UAA-β2m-2 and pCtid-UAA-β2m-1-II). Of note, in pCtid-UAA-β2m-2, a unique hydrogen bond network formed in the bottom of the peptide-binding groove (PBG) led to α2-helix drift, ultimately leading to structural changes in the PBG. The mechanism of the change in peptide presentation profiles by β2m molecules is illustrated. The results are also of great significance for antivirus and antitumor functions in cold-blooded vertebrates and even humans.
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