Summary for 4PP8
| Entry DOI | 10.2210/pdb4pp8/pdb |
| Descriptor | NKG2-D type II integral membrane protein, Retinoic acid early-inducible protein 1-beta, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | murine nk cell ligand, rae-1 beta, nkg2d, mhc-i platform, immune system |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Membrane; Single-pass type II membrane protein (By similarity): O54709 Cell membrane; Lipid-anchor, GPI-anchor: O08603 |
| Total number of polymer chains | 4 |
| Total formula weight | 68929.87 |
| Authors | Li, P.,Strong, R.K. (deposition date: 2014-02-26, release date: 2014-04-09, Last modification date: 2024-10-30) |
| 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 Cited by 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: 11825567PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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