The HIV capsid mimics karyopherin engagement with FG-nucleoporins. HIV can infect non-dividing cells by overcoming the nuclear pore complex (NPC) barrier, as its capsid is much larger than the diffusion limit. The NPC's central channel contains FG-rich nucleoporins that interact with karyopherins to facilitate transport. This study shows that the HIV capsid interacts with FG motifs in nucleoporins, enabling it to penetrate FG-nucleoporin condensates. This interaction resembles karyopherin behavior, allowing the capsid to bypass the NPC without destruction. The HIV capsid, containing multiple FG-binding sites, can engage with FG-repeat nucleoporins, enabling nuclear entry. The study used in vitro techniques to demonstrate that the HIV capsid binds to FG-repeat nucleoporins, including Nup98, which is a major contributor of FG motifs to the NPC. The capsid's FG-binding pocket interacts with specific FG motifs in nucleoporins, such as those in Nup153 and CPSF6. These interactions are crucial for nuclear entry, as mutations in the capsid's FG-binding sites affect its ability to infect non-dividing cells. The study also shows that the HIV capsid can enter FG-Nup condensates, demonstrating its ability to navigate the NPC. The findings suggest that the HIV capsid mimics karyopherin function, enabling it to enter the nucleus without being broken down. This mechanism may be conserved in other viruses and could have implications for viral infection and gene delivery. The study highlights the importance of FG interactions in nuclear transport and provides insights into how the HIV capsid interacts with the NPC.The HIV capsid mimics karyopherin engagement with FG-nucleoporins. HIV can infect non-dividing cells by overcoming the nuclear pore complex (NPC) barrier, as its capsid is much larger than the diffusion limit. The NPC's central channel contains FG-rich nucleoporins that interact with karyopherins to facilitate transport. This study shows that the HIV capsid interacts with FG motifs in nucleoporins, enabling it to penetrate FG-nucleoporin condensates. This interaction resembles karyopherin behavior, allowing the capsid to bypass the NPC without destruction. The HIV capsid, containing multiple FG-binding sites, can engage with FG-repeat nucleoporins, enabling nuclear entry. The study used in vitro techniques to demonstrate that the HIV capsid binds to FG-repeat nucleoporins, including Nup98, which is a major contributor of FG motifs to the NPC. The capsid's FG-binding pocket interacts with specific FG motifs in nucleoporins, such as those in Nup153 and CPSF6. These interactions are crucial for nuclear entry, as mutations in the capsid's FG-binding sites affect its ability to infect non-dividing cells. The study also shows that the HIV capsid can enter FG-Nup condensates, demonstrating its ability to navigate the NPC. The findings suggest that the HIV capsid mimics karyopherin function, enabling it to enter the nucleus without being broken down. This mechanism may be conserved in other viruses and could have implications for viral infection and gene delivery. The study highlights the importance of FG interactions in nuclear transport and provides insights into how the HIV capsid interacts with the NPC.