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- W1576221191 abstract "This chapter reviews the structure and functions of the human immunodeficiency virus type 1 (HIV‐1) nucleocapsid (NC) protein and discusses the rational for a simple, rapid screening of anti‐NC drugs aimed at inhibiting virion production. Retroviral nucleocapsid (NC) proteins are small proteins generated by the cleavage of the Gag structural polyprotein by the viral protease and are characterized by one or two copies of a highly conserved CCHC zinc finger (ZF) flanked by basic residues. Retroviral NC proteins are nucleic acid–binding proteins with potent RNA‐chaperoning properties, enabling important structural rearrangements that are required for genomic RNA replication and its packaging during virion assembly. The three‐dimensional (3D) conformation of HIV‐1 NC shows that the central domain folds into a hydrophobic plateau flanked by disordered basic sequences. The NC hydrophobic plateau pilots the selection, dimerization, and packaging of the genomic RNA during the virion assembly process, which ensures the formation of a mature functional inner capsid structure. The chapter describes a new one‐step screening assay, which allows for the rapid in vitro identification of anti‐NC compounds aimed at binding to the hydrophobic plateau, thus, inhibiting NC during the early and late steps of HIV‐1 replication." @default.
- W1576221191 created "2016-06-24" @default.
- W1576221191 creator A5054249539 @default.
- W1576221191 creator A5057462377 @default.
- W1576221191 creator A5083995281 @default.
- W1576221191 creator A5084052195 @default.
- W1576221191 creator A5091859966 @default.
- W1576221191 date "2007-01-01" @default.
- W1576221191 modified "2023-09-25" @default.
- W1576221191 title "Properties, Functions, and Drug Targeting of the Multifunctional Nucleocapsid Protein of the Human Immunodeficiency Virus" @default.
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