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The p24 protein of Human immunodeficiency virus type 1 is the major structural component of the viral capsid, forming a cone-shaped shell around the viral RNA genome. Encoded by the gag gene, p24 is composed of N-terminal and C-terminal domains linked flexibly and exists as pentamers or hexamers in assembled virions. Its structure has been extensively studied by X-ray crystallography and cryo-electron microscopy, revealing interactions between host factors such as cyclophilin A and regions critical for capsid morphology and infectivity. Though not considered a classical therapeutic target (such as enzymes or receptors), p24 is a promising focus for antiviral research due to its essential role in capsid assembly and viral replication. It is widely used as a diagnostic biomarker in early HIV infection and remains an important research subject for understanding virus-host interactions, capsid dynamics, and potential antiviral strategies.
Capsid destabilization or stabilization: Small molecules (e.g., PF74) bind to pockets within hexameric p24 and interfere with capsid integrity and virus replication
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