The HIV capsid can infect non-dividing cells by overcoming the selective barrier of the nuclear pore complex (NPC), which is composed of intrinsically disordered nucleoporin domains enriched in phenylalanine–glycine (FG) dipeptides. The HIV capsid, which is over 1,000 times larger than the size limit of the NPC diffusion barrier, interacts with multiple FG motifs from nucleoporins through a pocket on its surface. This interaction allows the capsid to penetrate FG-nucleoporin condensates, facilitating nuclear entry. The study used fluorescence fluctuation spectroscopy to screen for interactions between the HIV capsid and cellular proteins, identifying specific interactions with various nucleoporins. The HIV capsid's ability to bind FG motifs is similar to that of karyopherins, which can carry large cargoes through the NPC. The capsid's FG-binding pocket was shown to mediate its entry into Nup98 condensates, a key component of the NPC diffusion barrier. The capsid's integrity was maintained during this process, and it successfully partitioned into the condensates, demonstrating its intrinsic karyopherin-like properties. This study provides insights into how the HIV capsid can navigate the NPC and highlights the potential for therapeutic strategies targeting this interaction.The HIV capsid can infect non-dividing cells by overcoming the selective barrier of the nuclear pore complex (NPC), which is composed of intrinsically disordered nucleoporin domains enriched in phenylalanine–glycine (FG) dipeptides. The HIV capsid, which is over 1,000 times larger than the size limit of the NPC diffusion barrier, interacts with multiple FG motifs from nucleoporins through a pocket on its surface. This interaction allows the capsid to penetrate FG-nucleoporin condensates, facilitating nuclear entry. The study used fluorescence fluctuation spectroscopy to screen for interactions between the HIV capsid and cellular proteins, identifying specific interactions with various nucleoporins. The HIV capsid's ability to bind FG motifs is similar to that of karyopherins, which can carry large cargoes through the NPC. The capsid's FG-binding pocket was shown to mediate its entry into Nup98 condensates, a key component of the NPC diffusion barrier. The capsid's integrity was maintained during this process, and it successfully partitioned into the condensates, demonstrating its intrinsic karyopherin-like properties. This study provides insights into how the HIV capsid can navigate the NPC and highlights the potential for therapeutic strategies targeting this interaction.