ИСТИНА

Currently, special attention is pay to transmembrane proteins, such as ion channels and membrane receptors. From an applied point of view, membrane proteins (MP) are of interest as targets for medicines and as objects for biotechnological development. The family of Toll-Like Receptor (TLR) refers to the first type of membrane proteins. It (TLRs) play a critical role in innate immunity as the first line of host defense. The medical and biological significance of the TLR signaling is obvious, since the disregulation of the TLR system causes various autoimmune diseases and septic shock, and some therapeutic strategies targeting TLRs have already emerged. Despite the fact that the general scheme of the operation of TLR receptors were known and even there are structures of individual fragments for some proteins of this family, the detailed mechanism of signal transmission inside the cell remains unclear. To date, structural problems were solved using methods of cryoelectron microscopy, X-ray diffraction analysis and NMR spectroscopy, but NMR studies in environments simulating the membrane allow getting information about the structure of the protein, its mobility and changes directly in the process of interaction with other proteins or ligands. With such data it possible to construct an accurate model of MP functioning and describe the process of signal transmission into the cell. This work present result of bacterial expression, purification and assignment of NMR spectra of the intracellular domain of TLR1. The obtained data serves as a starting point for studying the mechanism of signal transmission inside the cell when TLR is activated.