Crystal structure of an HIV assembly and maturation switch
Copyright policy )Crystal structure of an HIV assembly and maturation switch
Virus assembly and maturation proceed through the programmed operation of molecular switches, which trigger both local and global structural rearrangements to produce infectious particles. HIV-1 contains an assembly and maturation switch that spans the C-terminal domain (CTD) of the capsid (CA) region and the first spacer peptide (SP1) of the precursor structural protein, Gag. The crystal structure of the CTD-SP1 Gag fragment is a goblet-shaped hexamer in which the cup comprises the CTD and an ensuing type II β-turn, and the stem comprises a 6-helix bundle. The β-turn is critical for immature virus assembly and the 6-helix bundle regulates proteolysis during maturation. This bipartite character explains why the SP1 spacer is a critical element of HIV-1 Gag but is not a universal property of retroviruses. Our results also indicate that HIV-1 maturation inhibitors suppress unfolding of the CA-SP1 junction and thereby delay access of the viral protease to its substrate.
- University of Virginia United States
- United States Department of State United States
- University of Virginia Health System United States
assembly, Models, Molecular, Protein Conformation, alpha-Helical, QH301-705.5, Science, Crystallography, X-Ray, Biochemistry, gag Gene Products, Human Immunodeficiency Virus, Capsid, Protein Domains, capsid, Escherichia coli, Amino Acid Sequence, Biology (General), Cloning, Molecular, Virus Assembly, Q, R, Virion, HIV, Recombinant Proteins, Proteolysis, HIV-1, Medicine, Capsid Proteins, Protein Conformation, beta-Strand, Protein Multimerization
assembly, Models, Molecular, Protein Conformation, alpha-Helical, QH301-705.5, Science, Crystallography, X-Ray, Biochemistry, gag Gene Products, Human Immunodeficiency Virus, Capsid, Protein Domains, capsid, Escherichia coli, Amino Acid Sequence, Biology (General), Cloning, Molecular, Virus Assembly, Q, R, Virion, HIV, Recombinant Proteins, Proteolysis, HIV-1, Medicine, Capsid Proteins, Protein Conformation, beta-Strand, Protein Multimerization
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