1JFM

CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA

Summary for 1JFM

• Entry DOI: 10.2210/pdb1jfm/pdb
• Descriptor: retinoic acid early transcript beta (2 entities in total)
• Functional Keywords: murine nk cell ligand, rae-1 beta, nkg2d, mhc-i platform, immune system
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: O08603
• Total number of polymer chains: 5
• Total formula weight: 100218.72

Authors

Li, P.,Strong, R.K. (deposition date: 2001-06-21, release date: 2002-02-20, Last modification date: 2024-11-20)

Primary citation

Li, P.,McDermott, G.,Strong, R.K.
Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D.
Immunity, 16:77-86, 2002

PubMed 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.

PubMed: 11825567
DOI: 10.1016/S1074-7613(02)00258-3

Experimental method

X-RAY DIFFRACTION (2.85 Å)