In Silico Modeling\nand Characterization of Epstein–Barr\nVirus Latent Membrane Protein 1 Protein

Latent membrane protein\n1 (LMP1) plays a crucial role in Epstein–Barr virus (EBV)’s\nability to establish latency and is involved in developing and progressing\nEBV-associated cancers. Additionally, EBV-infected cells affect the\nimmune responses, making it challenging for the immune system to eliminate\nthem. Due to the aforementioned reasons, it is crucial to understand\nthe structural features of LMP1, which are essential for the development\nof novel cancer therapies that target its signaling pathways. To date,\nthere is yet to be a complete LMP1 protein structure; therefore, in\nour work, we modeled the full-length LMP1 containing the short cytoplasmic\nN-terminus, six transmembrane domains (TMDs), and a long-simulated\nC-terminus. Our model showed good stability and protein compactness\nevaluated through accelerated-molecular dynamics, where the conformational\nensemble exhibited compact folds, particularly in the TMDs. Our results\nsuggest that specific domains or motifs, predominantly in the C-terminal\ndomain of LMP1, show promise as potential drug targets. As a whole,\nour work provides insights into key structural features of LMP1 that\nwill allow the development of novel LMP1 therapies.