3wyr | pdb_00003wyr

Crystal structure of Killer cell immunoglobulin-like receptor 2DL4

spinqualitylabelsall models 3wyr, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wyr is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Gene: KIR2DL4, CD158D, KIR103AS (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KI2L4_HUMAN] Receptor on natural killer (NK) cells for HLA-C alleles. Inhibits the activity of NK cells thus preventing cell lysis. Publication Abstract from PubMed The engagement of natural killer cell immunoglobulin-like receptors (KIRs) with their target ligands, human leukocyte antigen (HLA) molecules, is a critical component of innate immunity. Structurally, KIRs typically have either two (D1-D2) or three (D0-D1-D2) extracellular immunoglobulin domains, with the D1 and D2 domain recognizing the alpha1 and alpha2 helices of HLA, respectively, whereas the D0 domain of the KIR3DLs binds a loop region flanking the alpha1 helix of the HLA molecule. KIR2DL4 is distinct from other KIRs (except KIR2DL5) in that it does not contain a D1 domain and instead has a D0-D2 arrangement. Functionally, KIR2DL4 is also atypical in that, unlike all other KIRs, KIR2DL4 has both activating and inhibitory signaling domains. Here, we determined the 2.8 A crystal structure of the extracellular domains of KIR2DL4. Structurally, KIR2DL4 is reminiscent of other KIR2DL receptors, with the D0 and D2 adopting the C2-type immunoglobulin fold arranged with an acute elbow angle. However, KIR2DL4 self-associated via the D0 domain in a concentration-dependent manner and was observed as a tetramer in the crystal lattice by size exclusion chromatography, dynamic light scattering, analytical ultracentrifugation, and small angle x-ray scattering experiments. The assignment of residues in the D0 domain to forming the KIR2DL4 tetramer precludes an interaction with HLA akin to that observed for KIR3DL1. Accordingly, no interaction was observed to HLA by direct binding studies. Our data suggest that the unique functional properties of KIR2DL4 may be mediated by self-association of the receptor. The structure of the atypical killer cell immunoglobulin-like receptor, KIR2DL4.,Moradi S, Berry R, Pymm P, Hitchen C, Beckham SA, Wilce MC, Walpole NG, Clements CS, Reid HH, Perugini MA, Brooks AG, Rossjohn J, Vivian JP J Biol Chem. 2015 Apr 17;290(16):10460-71. doi: 10.1074/jbc.M114.612291. Epub, 2015 Mar 10. PMID:25759384 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NK cell receptor

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