5EFI

Crystal structure of mouse CD1d in complex with the p99p lipopeptide

5EFI の概要

• エントリーDOI: 10.2210/pdb5efi/pdb
• 関連するPDBエントリー: 5fkp
• 分子名称: Antigen-presenting glycoprotein CD1d1, OCTANOIC ACID (CAPRYLIC ACID), Beta-2-microglobulin, ... (11 entities in total)
• 機能のキーワード: cd1d, lipopeptide, alpha-helical peptide, immune system
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 49404.46

構造登録者

Girardi, E.,Wang, J.,Zajonc, D.M. (登録日: 2015-10-23, 公開日: 2016-03-30, 最終更新日: 2024-11-13)

主引用文献

Girardi, E.,Wang, J.,Zajonc, D.M.
Structure of an alpha-Helical Peptide and Lipopeptide Bound to the Nonclassical Major Histocompatibility Complex (MHC) Class I Molecule CD1d.
J.Biol.Chem., 291:10677-10683, 2016

PubMed Abstract: Mouse CD1d is a nonclassical MHC molecule able to present lipids and glycolipids to a specialized subset of T cells known as natural killer T cells. The antigens presented by CD1d have been shown to cover a broad range of chemical structures and to follow precise rules determining the potency of the antigen in the context of T cell activation. Together with lipids, initial reports suggested that CD1d can also bind and present hydrophobic peptides with (F/W)XX(I/L/M)XXW. However, the exact location of peptide binding and the molecular basis for the required motif are currently unknown. Here we present the crystal structure of the first peptide identified to bind CD1d, p99, and show that it binds in the antigen-binding groove of CD1d in a manner compatible with its presentation to T cell receptors. Interestingly, the peptide adopts an α-helical conformation, which orients the motif residues toward its deep binding groove, therefore explaining the molecular requirements for peptide binding. Moreover, we demonstrate that a lipopeptide version of the same peptide is able to bind CD1d in a similar conformation, identifying another class of molecules binding this antigen-presenting molecule.

PubMed: 27006394
DOI: 10.1074/jbc.M115.702118

実験手法

X-RAY DIFFRACTION (1.8 Å)