Structural highlights
Function
[KLRB1_HUMAN] Plays an inhibitory role on natural killer (NK) cells cytotoxicity. Activation results in specific acid sphingomyelinase/SMPD1 stimulation with subsequent marked elevation of intracellular ceramide. Activation also leads to AKT1/PKB and RPS6KA1/RSK1 kinases stimulation as well as markedly enhanced T-cell proliferation induced by anti-CD3. Acts as a lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal epitope as well as to the N-acetyllactosamine epitope. Binds also to CLEC2D/LLT1 as a ligand and inhibits NK cell-mediated cytotoxicity as well as interferon-gamma secretion in target cells.[1] [2] [3]
References
- ↑ Pozo D, Vales-Gomez M, Mavaddat N, Williamson SC, Chisholm SE, Reyburn H. CD161 (human NKR-P1A) signaling in NK cells involves the activation of acid sphingomyelinase. J Immunol. 2006 Feb 15;176(4):2397-406. PMID:16455998
- ↑ Christiansen D, Mouhtouris E, Milland J, Zingoni A, Santoni A, Sandrin MS. Recognition of a carbohydrate xenoepitope by human NKRP1A (CD161). Xenotransplantation. 2006 Sep;13(5):440-6. doi: 10.1111/j.1399-3089.2006.00332.x. PMID:16925668 doi:http://dx.doi.org/10.1111/j.1399-3089.2006.00332.x
- ↑ Lanier LL, Chang C, Phillips JH. Human NKR-P1A. A disulfide-linked homodimer of the C-type lectin superfamily expressed by a subset of NK and T lymphocytes. J Immunol. 1994 Sep 15;153(6):2417-28. PMID:8077657
