ArticleProceedings of the National Academy of Sciences of the United States of America2024
Structural insights into human MHC-II association with invariant chain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Article
- Article
- Methyl-CpG-binding domain protein 2 epigenetically represses monocyte HLA-DR expression and promotes immune paralysis in HBV-related acute-on-chronic liver failure.Frontiers in immunology · 2026Article
- A common network of residue-residue contacts underlies interactions between peptides and HLA class II complex.PloS one · 2026Article
- Review
- Uncovering the Genetic Basis of Porcine Resilience Through GWAS of Feed Intake Data.Animals : an open access journal from MDPI · 2025Article
- Astrocytic lipid droplets contain MHCII and may act as cogs in the antigen presentation machinery.Journal of neuroinflammation · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The loading of processed peptides on to major histocompatibility complex II (MHC-II) molecules for recognition by T cells is vital to cell-mediated adaptive immunity. As part of this process, MHC-II associates with the invariant chain (Ii) during biosynthesis in the endoplasmic reticulum to prevent premature peptide loading and to serve as a scaffold for subsequent proteolytic processing into MHC-II-CLIP. Cryo-electron microscopy structures of full-length Human Leukocyte Antigen-DR (HLA-DR) and HLA-DQ complexes associated with Ii, resolved at 3.0 to 3.1 Å, elucidate the trimeric assembly of the HLA/Ii complex and define atomic-level interactions between HLA, Ii transmembrane domains, loop domains, and class II-associated invariant chain peptides (CLIP). Together with previous structures of MHC-II peptide loading intermediates DO and DM, our findings complete the structural path governing class II antigen presentation.
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Registered trials
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