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| Title | Structural insights into human MHC-II association with invariant chain. |
|---|---|
| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 121, Issue 19, Page e2403031121, Year 2024 |
| Publish date | May 7, 2024 |
 Authors | Nan Wang / Deepa Waghray / Nathanael A Caveney / Kevin M Jude / K Christopher Garcia /  |
| PubMed 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 ...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. |
 External links | Proc Natl Acad Sci U S A / PubMed:38687785 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.03 - 3.12 Å |
| Structure data | EMDB-43488, PDB-8vrw: EMDB-43501, PDB-8vsp: |
| Chemicals |  ChemComp-NAG: |
| Source |
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 Keywords |  IMMUNE SYSTEM / Antigen presentation / membrane protein / trimeric complex |
