Abstract
Latent membrane protein 1 (LMP1) plays a crucial role in Epstein-Barr virus (EBV)'s ability to establish latency and is involved in developing and progressing EBV-associated cancers. Additionally, EBV-infected cells affect the immune responses, making it challenging for the immune system to eliminate them. Due to the aforementioned reasons, it is crucial to understand the structural features of LMP1, which are essential for the development of novel cancer therapies that target its signaling pathways. To date, there is yet to be a complete LMP1 protein structure; therefore, in our work, we modeled the full-length LMP1 containing the short cytoplasmic N-terminus, six transmembrane domains (TMDs), and a long-simulated C-terminus. Our model showed good stability and protein compactness evaluated through accelerated-molecular dynamics, where the conformational ensemble exhibited compact folds, particularly in the TMDs. Our results suggest that specific domains or motifs, predominantly in the C-terminal domain of LMP1, show promise as potential drug targets. As a whole, our work provides insights into key structural features of LMP1 that will allow the development of novel LMP1 therapies.