Structural highlights
Function
[NKG2D_MOUSE] Receptor for RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1. Involved in the immune surveillance exerted by T and B lymphocytes.[1] [RAE1B_MOUSE] Acts as a ligand for NKG2D.[2]
Publication Abstract from PubMed
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.
Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D.,Li P, McDermott G, Strong RK Immunity. 2002 Jan;16(1):77-86. PMID:11825567[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carayannopoulos LN, Naidenko OV, Fremont DH, Yokoyama WM. Cutting edge: murine UL16-binding protein-like transcript 1: a newly described transcript encoding a high-affinity ligand for murine NKG2D. J Immunol. 2002 Oct 15;169(8):4079-83. PMID:12370332
- ↑ Cerwenka A, Bakker AB, McClanahan T, Wagner J, Wu J, Phillips JH, Lanier LL. Retinoic acid early inducible genes define a ligand family for the activating NKG2D receptor in mice. Immunity. 2000 Jun;12(6):721-7. PMID:10894171
- ↑ Li P, McDermott G, Strong RK. Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D. Immunity. 2002 Jan;16(1):77-86. PMID:11825567
