We believe that the inability of Predikin to make predictions for these kinases is simply due to a lack of kinases with similar specificity-determining residues in PredikinDB, and that this will be rectified in time as our knowledge of BI-D1870 kinase-substrate interactions grows. Since the first successful kidney allo-transplantation in human beings in 1952, the development of treatments limiting acute allograft rejection has been the purpose of intense investigations. Even though the discovery of immunosuppressive molecules such as Cyclosporin A dramatically reduced acute allograft rejection cases, their action on chronic allograft rejection is not optimal. Moreover, besides their lack of efficiency on chronic allograft rejection, these immunosuppressive treatments have side effects including high susceptibility to infections, and renal and neural toxicity. Among the biological molecules involved in the induction of tolerance that have been characterized over the past years, the non-classical HLA class I Human Leukocyte Antigen G molecule has unique features that make it an ideal candidate for the development of new therapies in transplantation. HLA-G is characterized by seven isoforms which derive from the alternative splicing of a unique primary transcript, by a very low amount of polymorphism, and by an expression which is restricted to fetal trophoblast cells, adult epithelial thymic cells, cornea, erythroid and endothelial cell precursors, and pancreatic islets. HLA-G may also be pathologically expressed by non-rejected allografts, lesion-infiltrating antigen presenting cells during inflammatory diseases, and tumor tissues and their tumor infiltrating APC. HLA-G is further expressed by monocytes in multiple sclerosis, and by monocytes and T cells in viral infections. HLA-G is a potent tolerogenic molecule that strongly inhibits the function of immune cells. Indeed, HLA-G inhibits NK cell and cytotoxic T lymphocyte cytolytic activity, CD4+ T cell alloproliferative responses, T cell and NK cell ongoing proliferation, and dendritic cell maturation. Furthermore, HLA-G was shown to induce regulatory T cells. HLA-G mediates its functions by interacting with three inhibitory receptors: ILT2 which is expressed by B cells, some T cells, some NK cells and all monocytes/dendritic cells, ILT4 which is expressed by myeloid cells, and KIR2DL4 which is expressed by some peripheral and decidual NK cells. The efficiency of the HLA-G binding to its receptors and the delivery of potent inhibitory signals have been shown to depend on HLA-G dimerization. Biochemical studies indicate that HLAG dimerization occurs through disulfide-bond formation between unique cysteine residues localized in position 42 of the HLA-G alpha-1 domain. Point mutation of C42 in Serine, which leads to the exclusive expression of HLA-G monomers demonstrated that HLA-G dimers, but not HLA-G monomers.