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8VSP

Cryo-EM structure of human invariant chain in complex with HLA-DQ

Summary for 8VSP
Entry DOI10.2210/pdb8vsp/pdb
EMDB information43501
DescriptorHLA class II histocompatibility antigen, DQ alpha 1 chain, HLA class II histocompatibility antigen, DQ beta 1 chain, HLA class II histocompatibility antigen gamma chain, ... (4 entities in total)
Functional Keywordsantigen presentation, membrane protein, trimeric complex, immune system
Biological sourceHomo sapiens (human)
More
Total number of polymer chains9
Total formula weight301564.10
Authors
Wang, N.,Caveney, N.A.,Jude, K.M.,Garcia, K.C. (deposition date: 2024-01-24, release date: 2024-05-08, Last modification date: 2024-11-06)
Primary citationWang, N.,Waghray, D.,Caveney, N.A.,Jude, K.M.,Garcia, K.C.
Structural insights into human MHC-II association with invariant chain.
Proc.Natl.Acad.Sci.USA, 121:e2403031121-e2403031121, 2024
Cited by
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 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.
PubMed: 38687785
DOI: 10.1073/pnas.2403031121
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.12 Å)
Structure validation

227561

數據於2024-11-20公開中

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