1jfm | pdb_00001jfm

CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA

spinqualitylabelsall models 1jfm, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jfm is a 5 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.85Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RAE1B_MOUSE Acts as a ligand for NKG2D. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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