3B6S

Crystal Structure of hla-b*2705 Complexed with the Citrullinated Vasoactive Intestinal Peptide Type 1 Receptor (vipr) Peptide (residues 400-408)

3B6S の概要

• エントリーDOI: 10.2210/pdb3b6s/pdb
• 関連するPDBエントリー: 1of2 1ogt
• 分子名称: HLA class I histocompatibility antigen, B-27 alpha chain, Beta-2-microglobulin, VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1, ... (4 entities in total)
• 機能のキーワード: immune sistem-complex, mhc (major histocompatibility complex), hla-b*2705, glycoprotein, host-virus interaction, immune response, membrane, mhc i, polymorphism, transmembrane, ubl conjugation, disease mutation, glycation, immunoglobulin domain, pyrrolidone carboxylic acid, secreted, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P03989; Secreted . Note=(Microbial infection) In the presence of M: P61769
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45207.19

構造登録者

Beltrami, A.,Rossmann, M.,Fiorillo, M.T.,Sorrentino, R.,Saenger, W.,Ziegler, A.,Uchanska-Ziegler, A. (登録日: 2007-10-29, 公開日: 2008-07-22, 最終更新日: 2024-10-30)

主引用文献

Beltrami, A.,Rossmann, M.,Fiorillo, M.T.,Paladini, F.,Sorrentino, R.,Saenger, W.,Kumar, P.,Ziegler, A.,Uchanska-Ziegler, B.
Citrullination-dependent Differential Presentation of a Self-peptide by HLA-B27 Subtypes.
J.Biol.Chem., 283:27189-27199, 2008

PubMed Abstract: Inflammatory processes are accompanied by the posttranslational modification of certain arginine residues within proteins to yield citrulline, although it is largely unknown how this modification influences antigen presentation. We employed crystallographic and functional studies to investigate whether the exchange of arginine to citrulline affects the display of a peptide by two human major histocompatibility antigen class I subtypes, HLA-B(*)2705 and HLA-B(*)2709. Both differ only in residue 116 within the peptide binding groove despite their differential association with ankylosing spondylitis, an inflammatory rheumatic disorder. The crystal structures described here show that a modified self-peptide, pVIPR-U5 (RRKWURWHL; U = citrulline), is presented by the two HLA-B27 molecules in distinct conformations. These binding modes differ not only drastically from each other but also from the conformations exhibited by the non-citrullinated peptide in a given subtype. The differential reactivity of HLA-B27-restricted cytotoxic T cells with modified or unmodified pVIPR supports the structural findings and shows that the presentation of citrullinated peptides has the potential to influence immune responses.

PubMed: 18650441
DOI: 10.1074/jbc.M802818200

実験手法

X-RAY DIFFRACTION (1.8 Å)