ArticleJournal of the American Chemical Society2013
Magic angle spinning NMR reveals sequence-dependent structural plasticity, dynamics, and the spacer peptide 1 conformation in HIV-1 capsid protein assemblies.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Synthesis ofMagnetic resonance in chemistry : MRC · 2026Article
- Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations.Current opinion in structural biology · 2024Review
- Virus Structures and Dynamics by Magic-Angle Spinning NMR.Annual review of virology · 2021Review
- Integrative structural biology of HIV-1 capsid protein assemblies: combining experiment and computation.Current opinion in virology · 2021Review
- CryoET structures of immature HIV Gag reveal six-helix bundle.Communications biology · 2021Article
- Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR.Nature structural & molecular biology · 2020Article
- Effects of an HIV-1 maturation inhibitor on the structure and dynamics of CA-SP1 junction helices in virus-like particles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Improving the quality of oriented membrane protein spectra using heat-compensated separated local field experiments.Journal of biomolecular NMR · 2019Article
- Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'.Journal of biomolecular NMR · 2019Article
- Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies.The journal of physical chemistry. B · 2019Article
- Article
- Advances in instrumentation and methodology for solid-state NMR of biological assemblies.Journal of structural biology · 2019Review
- Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5α identified by magic-angle spinning NMR and molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.Journal of biomolecular NMR · 2018Article
- Quenching protein dynamics interferes with HIV capsid maturation.Nature communications · 2017Article
- Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz.Solid state nuclear magnetic resonance · 2017Article
- In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature.Scientific reports · 2017Article
- CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations.The journal of physical chemistry. B · 2017Article
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14 authors.
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Abstract
A key stage in HIV-1 maturation toward an infectious virion requires sequential proteolytic cleavage of the Gag polyprotein leading to the formation of a conical capsid core that encloses the viral RNA genome and a small complement of proteins. The final step of this process involves severing the SP1 peptide from the CA-SP1 maturation intermediate, which triggers the condensation of the CA protein into the capsid shell. The details of the overall mechanism, including the conformation of the SP1 peptide in CA-SP1, are still under intense debate. In this report, we examine tubular assemblies of CA and the CA-SP1 maturation intermediate using magic angle spinning (MAS) NMR spectroscopy. At magnetic fields of 19.9 T and above, outstanding quality 2D and 3D MAS NMR spectra were obtained for tubular CA and CA-SP1 assemblies, permitting resonance assignments for subsequent detailed structural characterization. Dipolar- and scalar-based correlation experiments unequivocally indicate that SP1 peptide is in a random coil conformation and mobile in the assembled CA-SP1. Analysis of two CA protein sequence variants reveals that, unexpectedly, the conformations of the SP1 tail, the functionally important CypA loop, and the loop preceding helix 8 are modulated by residue variations at distal sites. These findings provide support for the role of SP1 as a trigger of the disassembly of the immature CA capsid for its subsequent de novo reassembly into mature cores and establish the importance of sequence-dependent conformational plasticity in CA assembly.
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