4ZFZ

Crystal structure of rhesus macaque MHC class I molecule Mamu-B*098 complexed with myristoylated 5-mer lipopeptide derived from SIV Nef protein

4ZFZ の概要

• エントリーDOI: 10.2210/pdb4zfz/pdb
• 分子名称: Major histocompatibility complex class I, Beta-2-microglobulin, 5-mer lipopeptide from Protein Nef, ... (9 entities in total)
• 機能のキーワード: mhc, lipopeptide, antigen presentation, aids, immune system
• 由来する生物種: Macaca mulatta (Rhesus macaque); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 181765.17

構造登録者

Morita, D.,Sugita, M. (登録日: 2015-04-22, 公開日: 2016-01-13, 最終更新日: 2024-11-20)

主引用文献

Morita, D.,Yamamoto, Y.,Mizutani, T.,Ishikawa, T.,Suzuki, J.,Igarashi, T.,Mori, N.,Shiina, T.,Inoko, H.,Fujita, H.,Iwai, K.,Tanaka, Y.,Mikami, B.,Sugita, M.
Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex
Nat Commun, 7:10356-10356, 2016

PubMed Abstract: The covalent conjugation of a 14-carbon saturated fatty acid (myristic acid) to the amino-terminal glycine residue is critical for some viral proteins to function. This protein lipidation modification, termed N-myristoylation, is targeted by host cytotoxic T lymphocytes (CTLs) that specifically recognize N-myristoylated short peptides; however, the molecular mechanisms underlying lipopeptide antigen (Ag) presentation remain elusive. Here we show that a primate major histocompatibility complex (MHC) class I-encoded protein is capable of binding N-myristoylated 5-mer peptides and presenting them to specific CTLs. A high-resolution X-ray crystallographic analysis of the MHC class I:lipopeptide complex reveals an Ag-binding groove that is elaborately constructed to bind N-myristoylated short peptides rather than prototypic 9-mer peptides. The identification of lipopeptide-specific, MHC class I-restricted CTLs indicates that the widely accepted concept of MHC class I-mediated presentation of long peptides to CTLs may need some modifications to incorporate a novel MHC class I function of lipopeptide Ag presentation.

PubMed: 26758274
DOI: 10.1038/ncomms10356

実験手法

X-RAY DIFFRACTION (1.763 Å)