Human immunodeficiency virus type 1 nucleocapsid protein 7 (NCp7)

Human immunodeficiency virus type 1 nucleocapsid protein 7 (NCp7) is a small, highly basic protein of ~55–72 amino acids generated by proteolytic processing of the HIV-1 Gag polyprotein[1][3]. It contains two zinc finger motifs of the Cys-X2-Cys-X4-His-X4-Cys type, and functions as a nucleic acid chaperone crucial for almost all stages of the viral replication cycle, including packaging and dimerization of the viral genome, annealing and unwinding of nucleic acids, and initiation of reverse transcription[1][3][5]. NCp7 binds single-stranded, GU-rich nucleic acids, facilitates the unfolding of stable RNA structures (such as G-quadruplexes) to allow reverse transcription, and is essential for correct encapsidation of the HIV RNA genome[2][3][4]. Its unique structure and function make it an attractive antiviral target, though no inhibitors have reached clinical use due to selectivity and safety challenges[2].

Other names

HIV-1 nucleocapsid proteinHIV nucleocapsid protein NCp7NCp7HIV-1 NC

Inhibitors generally act via zinc finger disruption or nucleotide/nucleic acid binding interference, impeding RNA chaperone activity and thereby blocking reverse transcription or viral assembly[2][3]