5WL1

Crystal Structure of Human CD1b in Complex with PG

5WL1 の概要

• エントリーDOI: 10.2210/pdb5wl1/pdb
• 分子名称: T-cell surface glycoprotein CD1b, 1,2-ETHANEDIOL, (19S,22R,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22lambda~5~-phosphahexacosan-19-yl (9E)-octadec-9-enoate, ... (12 entities in total)
• 機能のキーワード: antigen presenting molecule, pg, phospholipid, mhc, cd1b, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49858.12

構造登録者

Shahine, A.,Gras, S.,Rossjohn, J. (登録日: 2017-07-25, 公開日: 2017-11-01, 最終更新日: 2024-10-23)

主引用文献

Shahine, A.,Van Rhijn, I.,Cheng, T.Y.,Iwany, S.,Gras, S.,Moody, D.B.,Rossjohn, J.
A molecular basis of human T cell receptor autoreactivity toward self-phospholipids.
Sci Immunol, 2:-, 2017

PubMed Abstract: Human T cell autoreactivity toward lipid antigens presented by CD1 proteins can manifest in numerous diseases, including psoriasis, contact hypersensitivities, and allergies. However, the molecular mechanisms for regulating T cell autoreactivity toward lipid antigens remain unclear. We determined the basis for T cell receptor (TCR) autoreactivity toward CD1b bound to self-phospholipids. The spectrum of self-antigens captured by CD1b skews toward abundant membrane phospholipids such as phosphatidylcholine and phosphatidylethanolamine. However, TCRs can specifically recognize rare phospholipids, including phosphatidylglycerol (PG). The structure of an autoreactive TCR bound to CD1b-PG shows that discrimination occurs through a marked induced fit movement of PG so that its polar head group fits snugly into the cationic cup of the TCR. Conversely, TCR binding toward ubiquitous self-phospholipids was sterically or electrostatically repelled. Accordingly, we describe a mechanism of TCR autoreactivity toward rare phospholipids and avoidance of autoreactivity to the most abundant self-phospholipids.

PubMed: 29054999
DOI: 10.1126/sciimmunol.aao1384

実験手法

X-RAY DIFFRACTION (1.38 Å)