ArticleProceedings of the National Academy of Sciences of the United States of America2007
Domain-swapped dimerization of the HIV-1 capsid C-terminal domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 97 citations in OpenAlex.
- Positive correlation between structural disorder of the HIV-1 Gag N-terminal segment and progeny virus particle formation.Journal of virology · 2025Article
- Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- The HIV-1 Gag Protein Displays Extensive Functional and Structural Roles in Virus Replication and Infectivity.International journal of molecular sciences · 2022Review
- Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.PloS one · 2021Article
- Mechanisms of PI(4,5)P2 Enrichment in HIV-1 Viral Membranes.Journal of molecular biology · 2020Article
- Critical Role of the Human T-Cell Leukemia Virus Type 1 Capsid N-Terminal Domain for Gag-Gag Interactions and Virus Particle Assembly.Journal of virology · 2018Article
- Fate of the Urinary Tract Virus BK Human Polyomavirus in Source-Separated Urine.Applied and environmental microbiology · 2018Article
- Amino-acid composition after loop deletion drives domain swapping.Protein science : a publication of the Protein Society · 2017Article
- Structure of FIV capsid C-terminal domain demonstrates lentiviral evasion of genetic fragility by coevolved substitutions.Scientific reports · 2016Article
- Mutations of Conserved Residues in the Major Homology Region Arrest Assembling HIV-1 Gag as a Membrane-Targeted Intermediate Containing Genomic RNA and Cellular Proteins.Journal of virology · 2016Article
- Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies.The journal of physical chemistry. B · 2016Article
- MAS NMR of HIV-1 protein assemblies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Biophysical analysis of the MHR motif in folding and domain swapping of the HIV capsid protein C-terminal domain.Biophysical journal · 2015Article
- How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Virus research · 2014Review
- CryoEM analysis of capsid assembly and structural changes upon interactions with a host restriction factor, TRIM5α.Methods in molecular biology (Clifton, N.J.) · 2014Article
- A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Tubular crystals and helical arrays: structural determination of HIV-1 capsid assemblies using iterative helical real-space reconstruction.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Article
- The effect of chemical chaperones on the assembly and stability of HIV-1 capsid protein.PloS one · 2013Article
- Dual role for motif 1 residues of human lysyl-tRNA synthetase in dimerization and packaging into HIV-1.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Assembly of the HIV and other retroviruses is primarily driven by the oligomerization of the Gag polyprotein, the major viral structural protein capable of forming virus-like particles even in the absence of all other virally encoded components. Several critical determinants of Gag oligomerization are located in the C-terminal domain of the capsid protein (CA-CTD), which encompasses the most conserved segment in the highly variable Gag protein called the major homology region (MHR). The CA-CTD is thought to function as a dimerization module, although the existing model of CA-CTD dimerization does not readily explain why the conserved residues of the MHR are essential for retroviral assembly. Here we describe an x-ray structure of a distinct domain-swapped variant of the HIV-1 CA-CTD dimer stabilized by a single amino acid deletion. In the domain-swapped structure, the MHR-containing segment forms a major part of the dimerization interface, providing a structural mechanism for the enigmatic function of the MHR in HIV assembly. Our observations suggest that swapping of the MHR segments of adjacent Gag molecules may be a critical intermediate in retroviral assembly.
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