Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D.
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.
Li
Pingwei
P
Fred Hutchinson Cancer Research Center, Division of Basic Sciences, Seattle, WA 98109, USA.
McDermott
Gerry
G
Strong
Roland K
RK
D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D006031:Glycosylation; D008565:Membrane Proteins / Q000737:chemistry*; D051379:Mice; D055655:NK Cell Lectin-Like Receptor Subfamily K; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011971:Receptors, Immunologic / Q000737:chemistry*; D055607:Receptors, Natural Killer Cell
C527085:KLRK1 protein, human; C527086:Klrk1 protein, mouse; D008565:Membrane Proteins; D055655:NK Cell Lectin-Like Receptor Subfamily K; C491219:Raet1a protein, mouse; C491218:Raet1b protein, mouse; D011971:Receptors, Immunologic; D055607:Receptors, Natural Killer Cell