ИСТИНА

NRADD (also called p45) is a 25kDa co-receptor of the p75 neurotrophin receptor. It associates with  the p75 and inhibits its activity. In this work, we solved the spatial structure and studied mobility of the NRADD in lipidic bicelles using solution nuclear magnetic resonance spectroscopy techniques. The structure is homologues to the p75NTR and represents relatively short unstructured N-terminal segment, followed by the α-helical transmembrane domain, extended intrinsically disordered chopper domain and C-terminal classic death domain. The flexibility of the juxtamembrane chopper domain does not impede free motion of the death domain, the fact that is required for the protein activity and should be explained. This study represents the first of its kind spatial structure of the full-length type I receptor, i.e. single-span membrane protein, obtained using nuclear magnetic resonance spectroscopy in solution. The work was supported by the Russian Science Foundation (grant #14-14-00573).