Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D. Academic Article uri icon

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.

published proceedings

  • Immunity

altmetric score

  • 6

author list (cited authors)

  • Li, P., McDermott, G., & Strong, R. K.

citation count

  • 90

complete list of authors

  • Li, Pingwei||McDermott, Gerry||Strong, Roland K

publication date

  • January 2002