4pp8 | pdb_00004pp8

Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D

spinqualitylabelsall models 4pp8, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pp8 is a 4 chain structure with sequence from Lk3 transgenic mice. This structure supersedes the now removed PDB entry 1jsk. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Gene: Klrk1, Nkg2d, RAE-1 BETA (LK3 transgenic mice), NKG2D, Raet1b (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NKG2D_MOUSE] Receptor for RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1. Involved in the immune surveillance exerted by T and B lymphocytes. [RAE1B_MOUSE] Acts as a ligand for NKG2D. 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. See Also NK cell receptor

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