4PP8

Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D

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4PP8 の概要

• エントリーDOI: 10.2210/pdb4pp8/pdb
• 分子名称: NKG2-D type II integral membrane protein, Retinoic acid early-inducible protein 1-beta, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: murine nk cell ligand, rae-1 beta, nkg2d, mhc-i platform, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type II membrane protein (By similarity): O54709; Cell membrane; Lipid-anchor, GPI-anchor: O08603
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68929.87

構造登録者

Li, P.,Strong, R.K. (登録日: 2014-02-26, 公開日: 2014-04-09, 最終更新日: 2024-10-30)

主引用文献

Li, P.,McDermott, G.,Strong, R.K.
Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D.
Immunity, 16:77-86, 2002

PubMed Abstract: Induced by retinoic acid and implicated in playing a role in development, rodent RAE-1 proteins are ligands for the activating immunoreceptor NKG2D, widely expressed on natural killer cells, T cells, and macrophages. RAE-1 proteins (alpha, beta, gamma, and delta) are distant major histocompatibility complex (MHC) class I homologs, comprising isolated alpha1alpha2 platform domains. The crystal structure of RAE-1beta was distorted from other MHC homologs and displayed noncanonical disulfide bonds. The loss of any remnant of a peptide binding groove was facilitated by the close approach of the groove-defining helices through a hydrophobic, leucine-rich interface. The RAE-1beta-murine NKG2D complex structure resembled the human NKG2D-MICA receptor-ligand complex and further demonstrated the promiscuity of the NKG2D ligand binding site.

PubMed: 11825567

実験手法

X-RAY DIFFRACTION (1.95 Å)