ArticleStructure (London, England : 1993)2013
Conformational transition of membrane-associated terminally acylated HIV-1 Nef.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Who cites it
19 citing papers in PubMed.
- Neutron Reflectometry and Molecular Simulations Demonstrate HIV-1 Nef Homodimer Formation on Model Lipid Bilayers.Journal of molecular biology · 2023Article
- Review
- Hydrogen/Deuterium Exchange Behavior During Denaturing/Refolding Processes Determined in Tetragonal Hen Egg-White Lysozyme Crystals.Molecular biotechnology · 2022Article
- Structure, function, and inhibitor targeting of HIV-1 Nef-effector kinase complexes.The Journal of biological chemistry · 2020Review
- Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Information gain from isotopic contrast variation in neutron reflectometry on protein-membrane complex structures.Journal of applied crystallography · 2020Article
- Membrane Anchoring of Hck Kinase via the Intrinsically Disordered SH4-U and Length Scale Associated with Subcellular Localization.Journal of molecular biology · 2020Article
- How HIV Nef Proteins Hijack Membrane Traffic To Promote Infection.Journal of virology · 2019Review
- Sensitivity of peripheral membrane proteins to the membrane context: A case study of phosphatidylserine and the TIM proteins.Biochimica et biophysica acta. Biomembranes · 2018Review
- Antiretroviral Drugs Alter the Content of Extracellular Vesicles from HIV-1-Infected Cells.Scientific reports · 2018Article
- Remodeling of HIV-1 Nef Structure by Src-Family Kinase Binding.Journal of molecular biology · 2018Article
- Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3.Nature communications · 2017Article
- Interaction Between HIV-1 Nef and Calnexin: From Modeling to Small Molecule Inhibitors Reversing HIV-Induced Lipid Accumulation.Arteriosclerosis, thrombosis, and vascular biology · 2016Article
- Hydrogen Exchange Mass Spectrometry of Proteins at Langmuir Monolayers.Analytical chemistry · 2015Article
- Membrane-Associated Conformation of HIV-1 Nef Investigated with Hydrogen Exchange Mass Spectrometry at a Langmuir Monolayer.Analytical chemistry · 2015Article
- Membrane association of the PTEN tumor suppressor: neutron scattering and MD simulations reveal the structure of protein-membrane complexes.Methods (San Diego, Calif.) · 2015Review
- Zooming in on disordered systems: neutron reflection studies of proteins associated with fluid membranes.Biochimica et biophysica acta · 2014Review
- Heterologous Src homology 4 domains support membrane anchoring and biological activity of HIV-1 Nef.The Journal of biological chemistry · 2014Article
- Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody.Retrovirology · 2014Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Many proteins are posttranslationally modified by acylation targeting them to lipid membranes. While methods such as X-ray crystallography and nuclear magnetic resonance are available to determine the structure of folded proteins in solution, the precise position of folded domains relative to a membrane remains largely unknown. We used neutron and X-ray reflection methods to measure the displacement of the core domain of HIV Nef from lipid membranes upon insertion of the N-terminal myristate group. Nef is one of several HIV-1 accessory proteins and an essential factor in AIDS progression. Upon insertion of the myristate and residues from the N-terminal arm, Nef transitions from a closed-to-open conformation that positions the core domain 70 Å from the lipid headgroups. This work rules out previous speculation that the Nef core remains closely associated with the membrane to optimize interactions with the cytoplasmic domain of MHC-1.
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