5DEG

Crystal structure of B*27:06 bound to the pVIPR peptide

5DEG の概要

• エントリーDOI: 10.2210/pdb5deg/pdb
• 関連するPDBエントリー: 1OF2 1OGT
• 分子名称: MHC class I antigen, Beta-2-microglobulin, Peptide derived of VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1 (pVIPR), ... (5 entities in total)
• 機能のキーワード: immune system-complex, immune system, mhc major histocompatibility complex), hla- b*2706
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45404.37

構造登録者

Loll, B.,Fabian, H.,Hee, C.S.,Huser, H.,Uchanska-Ziegler, B.,Ziegler, A. (登録日: 2015-08-25, 公開日: 2015-11-18, 最終更新日: 2024-10-23)

主引用文献

Loll, B.,Fabian, H.,Huser, H.,Hee, C.S.,Ziegler, A.,Uchanska-Ziegler, B.,Ziegler, A.
Increased Conformational Flexibility of HLA-B*27 Subtypes Associated With Ankylosing Spondylitis.
Arthritis Rheumatol, 68:1172-1182, 2016

PubMed Abstract: Dissimilarities in antigen processing and presentation are known to contribute to the differential association of HLA-B*27 subtypes with the inflammatory rheumatic disease ankylosing spondylitis (AS). In support of this notion, previous x-ray crystallographic data showed that peptides can be displayed by almost identical HLA-B*27 molecules in a subtype-dependent manner, allowing cytotoxic T lymphocytes to distinguish between these subtypes. For example, a human self-peptide derived from vasoactive intestinal peptide receptor type 1 (pVIPR; sequence RRKWRRWHL) is displayed in a single conformation by B*27:09 (which is not associated with AS), while B*27:05 (which is associated with AS) presents the peptide in a dual binding mode. In addition, differences in conformational flexibility between these subtypes might affect their stability or antigen presentation capability. This study was undertaken to investigate B*27:04 and B*27:06, another pair of minimally distinct HLA-B*27 subtypes, to assess whether dual peptide conformations or structural dynamics play a role in the initiation of AS.

PubMed: 26748477
DOI: 10.1002/art.39567

実験手法

X-RAY DIFFRACTION (1.83 Å)