HIV-1 integrase (IN) must cross the nuclear envelope to access the host genome and catalyze viral DNA integration, a process that requires active nuclear import. While several host nuclear import factors have been implicated in this step, importin 7 (Imp7) has emerged as a particularly strong candidate. However, its precise role and the molecular details of its interaction with IN were unclear. Here, we demonstrate that Imp7 is a critical mediator of IN nuclear import. Using hydrogen-deuterium exchange and cross-linking mass spectrometry methods, we identify the core domain of Imp7 as the IN-binding site. Affinity measurements show that IN binds Imp7 with high affinity, and that mutations within the C-terminal nuclear localization signal (NLS) of IN markedly reduce this interaction. Moreover, Imp7 knockdown in HEK293 cells results in cytoplasmic accumulation of IN, confirming its essential role in nuclear import. These findings establish a direct, high-affinity interaction between IN and Imp7, define their molecular interface, and identify Imp7 as a key nuclear import receptor for HIV-1 IN. These results provide detailed molecular insight into a critical host-virus interaction during early HIV-1 replication and indicate that the IN C-terminal domain-Imp7 interface is a promising target for therapeutic strategies. In this context, disrupting this interaction with small molecules or peptides could block the nuclear import of integrase, thereby delaying infection and providing a complementary antiviral strategy to the current integrase inhibitors.