About: LILRA2 is a research topic. Over the lifetime, 6 publications have been published within this topic receiving 65 citations. The topic is also known as: CD85H & ILT1.
TL;DR: The LILRA2 extracellular D1D2 domain crystal structure is reported, which reveals structural shifts of the corresponding MHC-binding amino acid residues in comparison with LILR B1/B2, explaining its non-binding to MHC molecules.
TL;DR: The large-scale stable production of ILT1 D1D2 domains is reported through engineering of site-directed mutagenesis that introduces a cysteine at amino acid position 142 to form a disulfide bond with the spare cys132 without topological influences of the native protein based on the known structures of the homologous ILT 2/4/11.
TL;DR: In this article, the authors proposed a method to solve the problem of artificial neural networks in the context of artificial intelligence, which is based on the work of the National Natural Science Foundation of China (NSFC).
Abstract: Ministry of Science and Technology (MOST) of China [2006CB504204]; National Natural Science Foundation (NSFC) of China [30671903
TL;DR: This chapter focuses on LILRs and, in particular, on their function during cytomegalovirus (CMV) infection and their ability to regulate adaptive responses during bacterial infection and following organ transplantation.
Abstract: To achieve self-tolerance, many inhibitory receptors recognize major histocompatibility complex class I (MHC-I) molecules, which are normally expressed on healthy cells. In humans, inhibitory MHC-I receptors include the killer cell immunoglobulin (Ig)-like receptors (KIRs), the leukocyte Ig-like receptors (LILRs), and the CD94/NKG2A heterodimer. This chapter focuses on LILRs and, in particular, on their function during cytomegalovirus (CMV) infection and their ability to regulate adaptive responses during bacterial infection and following organ transplantation. The members of the LILR family--also known as immunoglobulin-like transcript (ILT), leukocyte Ig-like receptor (LIR), monocyte and macrophage Ig-like receptor (MIR), or CD85--include at least 11 distinct molecules, which have either two or four homologous extracellular Ig-like domains of the C2 type. Inhibitory LILRs (LILRB1, LILRB2, LILRB3, LILRB4, and LILRB5) contain long cytoplasmic domains with two to four immunoreceptor tyrosine-based inhibitory motifs (ITIMs). Another group of LILRs (LILRA1, LILRA2, ILT7, ILT8, and ILT11) have short cytoplasmic domains that lack ITIMs or recognizable docking motifs for signaling mediators. If LILRs have evolved under the selective pressure of UL18, one would also expect that UL18 mutates to neutralize this strategy of the host immune system. A recent study suggests that the ability of inhibitory LILRs to regulate the function of antigen-presenting cells (APCs) may be an important mechanism utilized by suppressor T (Ts) cells to induce immunological tolerance.