1jfm
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| , resolution 2.85Å | |||||||
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| Gene: | RAE-1beta (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA
OverviewOverview
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.
About this StructureAbout this Structure
1JFM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Mar 30 21:32:58 2008