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Updated: Aug 22, 2026

A Protocol for the Production of KLRG1 Tetramer
Published on: January 12, 2010
Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D
Pingwei Li1, Gerry McDermott, Roland K Strong
1Fred Hutchinson Cancer Research Center, Division of Basic Sciences, Seattle, WA 98109, USA.
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.
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