ArticleThe Journal of biological chemistry2016
Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Synthesis ofMagnetic resonance in chemistry : MRC · 2026Article
- LoCoHD: a metric for comparing local environments of proteins.Nature communications · 2024Article
- Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations.Current opinion in structural biology · 2024Review
- Changes in dynamic and static structures of the HIV-1 p24 capsid protein N-domain caused by amino-acid substitution are associated with its viral viability.Protein science : a publication of the Protein Society · 2021Article
- Virus Structures and Dynamics by Magic-Angle Spinning NMR.Annual review of virology · 2021Review
- Curvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch.The journal of physical chemistry letters · 2021Article
- Review
- Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.Biochimica et biophysica acta. Biomembranes · 2020Article
- Article
- Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.Journal of biomolecular NMR · 2018Article
- Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.The journal of physical chemistry. B · 2018Article
- Helical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles.Journal of the American Chemical Society · 2016Article
- Structure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular Assemblies.Journal of the American Chemical Society · 2016Article
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Abstract
We present the results of solid state nuclear magnetic resonance (NMR) experiments on HIV-1 capsid protein (CA) assemblies with three different morphologies, namely wild-type CA (WT-CA) tubes with 35-60 nm diameters, planar sheets formed by the Arg(18)-Leu mutant (R18L-CA), and R18L-CA spheres with 20-100 nm diameters. The experiments are intended to elucidate molecular structural variations that underlie these variations in CA assembly morphology. We find that multidimensional solid state NMR spectra of (15)N,(13)C-labeled CA assemblies are remarkably similar for the three morphologies, with only small differences in (15)N and (13)C chemical shifts, no significant differences in NMR line widths, and few differences in the number of detectable NMR cross-peaks. Thus, the pronounced differences in morphology do not involve major differences in the conformations and identities of structurally ordered protein segments. Instead, morphological variations are attributable to variations in conformational distributions within disordered segments, which do not contribute to the solid state NMR spectra. Variations in solid state NMR signals from certain amino acid side chains are also observed, suggesting differences in the intermolecular dimerization interface between curved and planar CA lattices, as well as possible differences in intramolecular helix-helix packing.
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