6C15

CD1c in complex with phosphatidylcholine

6C15 の概要

• エントリーDOI: 10.2210/pdb6c15/pdb
• 関連するPDBエントリー: 6C09
• 分子名称: T-cell surface glycoprotein CD1c, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Beta-2-microglobulin, ... (11 entities in total)
• 機能のキーワード: antigen presentation, 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: 46980.81

構造登録者

Wun, K.S.,Rossjohn, J. (登録日: 2018-01-03, 公開日: 2018-03-21, 最終更新日: 2023-10-04)

主引用文献

Wun, K.S.,Reijneveld, J.F.,Cheng, T.Y.,Ladell, K.,Uldrich, A.P.,Le Nours, J.,Miners, K.L.,McLaren, J.E.,Grant, E.J.,Haigh, O.L.,Watkins, T.S.,Suliman, S.,Iwany, S.,Jimenez, J.,Calderon, R.,Tamara, K.L.,Leon, S.R.,Murray, M.B.,Mayfield, J.A.,Altman, J.D.,Purcell, A.W.,Miles, J.J.,Godfrey, D.I.,Gras, S.,Price, D.A.,Van Rhijn, I.,Moody, D.B.,Rossjohn, J.
T cell autoreactivity directed toward CD1c itself rather than toward carried self lipids.
Nat. Immunol., 19:397-406, 2018

PubMed Abstract: The hallmark function of αβ T cell antigen receptors (TCRs) involves the highly specific co-recognition of a major histocompatibility complex molecule and its carried peptide. However, the molecular basis of the interactions of TCRs with the lipid antigen-presenting molecule CD1c is unknown. We identified frequent staining of human T cells with CD1c tetramers across numerous subjects. Whereas TCRs typically show high specificity for antigen, both tetramer binding and autoreactivity occurred with CD1c in complex with numerous, chemically diverse self lipids. Such extreme polyspecificity was attributable to binding of the TCR over the closed surface of CD1c, with the TCR covering the portal where lipids normally protrude. The TCR essentially failed to contact lipids because they were fully seated within CD1c. These data demonstrate the sequestration of lipids within CD1c as a mechanism of autoreactivity and point to small lipid size as a determinant of autoreactive T cell responses.

PubMed: 29531339
DOI: 10.1038/s41590-018-0065-7

実験手法

X-RAY DIFFRACTION (3.21 Å)