Rabies virus is a non-segmented negative sense RNA virus that causes encephalitis in humans with a 100% case fatality rate, resulting in > 61,000 deaths/year world-wide. There are currently no treatments for rabies disease, but a number of critical interactions of viral proteins provide potential targets to develop new antiviral compounds. The RNA polymerase of rabies virus consists of two subunits, the large (L) protein and the phosphoprotein. The binding of L to P forms the RdRP complex and is thought to help position L to gain access to the RNA bases of the N–RNA template. While the RNA-dependent RNA polymerase L protein of rabies virus (RABV) has potential to be a therapeutic target for rabies, the molecular functions of this protein have remained largely unknown. In addition, the research findings showed that the amino acid sequence at positions 1,929-1,933 (NPYNE) of L protein is functionally important for binding of the L protein with its essential cofactor P protein, thereby also for L protein’s RNA polymerase activity. In this study, we aim to investigate the structure of P and L protein of Rabies Virus using CryoEM and NMR. Knowledge about the structure and function of rabies protein complexes will help in designing new drugs for treatment of rabies.