NKG2-F type II integral membrane protein is a protein that in humans is encoded by the KLRC4gene.
Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. NK cells preferentially express several calcium-dependent (C-type) lectins, which have been implicated in the regulation of NK cell function. KLRC4 is a member of the NKG2 group which are expressed primarily in natural killer (NK) cells and encodes a family of transmembrane proteins characterized by a type II membrane orientation (extracellular C terminus) and the presence of a C-type lectin domain. The NKG2 gene family is located within the NK complex, a region that contains several C-type lectin genes preferentially expressed on NK cells. The 3' end of the KLRC4 transcript includes the first non-coding exon found at the 5' end of the adjacent D12S2489E gene transcript.
Yabe T, McSherry C, Bach FH, et al. (1993). "A multigene family on human chromosome 12 encodes natural killer-cell lectins". Immunogenetics37 (6): 455–60. doi:10.1007/BF00222470. PMID8436421.
Plougastel B, Trowsdale J (1998). "Cloning of NKG2-F, a new member of the NKG2 family of human natural killer cell receptor genes". Eur. J. Immunol.27 (11): 2835–9. doi:10.1002/eji.1830271114. PMID9394807.
Glienke J, Sobanov Y, Brostjan C, et al. (1998). "The genomic organization of NKG2C, E, F, and D receptor genes in the human natural killer gene complex". Immunogenetics48 (3): 163–73. doi:10.1007/s002510050420. PMID9683661.
Li P, Morris DL, Willcox BE, et al. (2001). "Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA". Nat. Immunol.2 (5): 443–51. doi:10.1038/87757. PMID11323699.
O'Callaghan CA, Cerwenka A, Willcox BE, et al. (2001). "Molecular competition for NKG2D: H60 and RAE1 compete unequally for NKG2D with dominance of H60". Immunity15 (2): 201–11. doi:10.1016/S1074-7613(01)00187-X. PMID11520456.
Radaev S, Rostro B, Brooks AG, et al. (2002). "Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3". Immunity15 (6): 1039–49. doi:10.1016/S1074-7613(01)00241-2. PMID11754823.
Sutherland CL, Chalupny NJ, Schooley K, et al. (2002). "UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D and activate multiple signaling pathways in primary NK cells". J. Immunol.168 (2): 671–9. doi:10.4049/jimmunol.168.2.671. PMID11777960.
Holmes MA, Li P, Petersdorf EW, Strong RK (2002). "Structural studies of allelic diversity of the MHC class I homolog MIC-B, a stress-inducible ligand for the activating immunoreceptor NKG2D". J. Immunol.169 (3): 1395–400. doi:10.4049/jimmunol.169.3.1395. PMID12133964.
Gilfillan S, Ho EL, Cella M, et al. (2002). "NKG2D recruits two distinct adapters to trigger NK cell activation and costimulation". Nat. Immunol.3 (12): 1150–5. doi:10.1038/ni857. PMID12426564.
Diefenbach A, Tomasello E, Lucas M, et al. (2002). "Selective associations with signaling proteins determine stimulatory versus costimulatory activity of NKG2D". Nat. Immunol.3 (12): 1142–9. doi:10.1038/ni858. PMID12426565.
McFarland BJ, Kortemme T, Yu SF, et al. (2004). "Symmetry recognizing asymmetry: analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands". Structure11 (4): 411–22. doi:10.1016/S0969-2126(03)00047-9. PMID12679019.