8VSP
Cryo-EM structure of human invariant chain in complex with HLA-DQ
8VSP の概要
エントリーDOI | 10.2210/pdb8vsp/pdb |
EMDBエントリー | 43501 |
分子名称 | HLA 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) |
機能のキーワード | antigen presentation, membrane protein, trimeric complex, immune system |
由来する生物種 | Homo sapiens (human) 詳細 |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 301564.10 |
構造登録者 | Wang, N.,Caveney, N.A.,Jude, K.M.,Garcia, K.C. (登録日: 2024-01-24, 公開日: 2024-05-08, 最終更新日: 2024-11-06) |
主引用文献 | Wang, 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: 38687785DOI: 10.1073/pnas.2403031121 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.12 Å) |
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