Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D

Immunity. 2002 Jan;16(1):77-86. doi: 10.1016/s1074-7613(02)00258-3.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Crystallization
  • Glycosylation
  • Membrane Proteins / chemistry*
  • Mice
  • NK Cell Lectin-Like Receptor Subfamily K
  • Protein Folding
  • Protein Structure, Secondary
  • Receptors, Immunologic / chemistry*
  • Receptors, Natural Killer Cell


  • KLRK1 protein, human
  • Klrk1 protein, mouse
  • Membrane Proteins
  • NK Cell Lectin-Like Receptor Subfamily K
  • Raet1a protein, mouse
  • Raet1b protein, mouse
  • Receptors, Immunologic
  • Receptors, Natural Killer Cell

Associated data

  • PDB/1JFM
  • PDB/1JSK