ArticleBiochemistry2006
Conformational flexibility and strand arrangements of the membrane-associated HIV fusion peptide trimer probed by solid-state NMR spectroscopy.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
30 citing papers in PubMed, 50 citations in OpenAlex.
- Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infection.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Priming antibody responses to the fusion peptide in rhesus macaques.NPJ vaccines · 2024Article
- Overlapping Properties of the Short Membrane-Active Peptide BP100 With (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides.Frontiers in cellular and infection microbiology · 2021Article
- Cholesterol-Induced Conformational Change in the Sphingomyelin Headgroup.Biophysical journal · 2019Article
- Challenges and approaches to understand cholesterol-binding impact on membrane protein function: an NMR view.Cellular and molecular life sciences : CMLS · 2018Review
- REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Article
- pH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.Biochimica et biophysica acta · 2015Article
- Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state.Journal of molecular biology · 2014Article
- Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.The journal of physical chemistry. A · 2013Article
- Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.Journal of biomolecular NMR · 2013Article
- Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR.Journal of biomolecular NMR · 2013Article
- Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation.European biophysics journal : EBJ · 2012Article
- Solid-state NMR spectroscopy of protein complexes.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Article
- Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.European biophysics journal : EBJ · 2011Article
- Effect of the HIV-1 fusion peptide on the mechanical properties and leaflet coupling of lipid bilayers.New journal of physics · 2011Article
- Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.Biochemistry · 2010Article
- HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics.Journal of molecular biology · 2010Article
- Origins of resistance to the HIVgp41 viral entry inhibitor T20.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The human immunodeficiency virus (HIV) fusion peptide (HFP) is the N-terminal apolar region of the HIV gp41 fusion protein and interacts with target cell membranes and promotes membrane fusion. The free peptide catalyzes vesicle fusion at least to the lipid mixing stage and serves as a useful model fusion system. For gp41 constructs which lack the HFP, high-resolution structures show trimeric protein and suggest that at least three HFPs interact with the membrane with their C-termini in close proximity. In addition, previous studies have demonstrated that HFPs which are cross-linked at their C-termini to form trimers (HFPtr) catalyze fusion at a rate which is 15-40 times greater than that of non-cross-linked HFP. In the present study, the structure of membrane-associated HFPtr was probed with solid-state nuclear magnetic resonance (NMR) methods. Chemical shift and intramolecular (13)CO-(15)N distance measurements show that the conformation of the Leu-7 to Phe-11 region of HFPtr has predominant helical conformation in membranes without cholesterol and beta strand conformation in membranes containing approximately 30 mol % cholesterol. Interstrand (13)CO-(13)CO and (13)CO-(15)N distance measurements were not consistent with an in-register parallel strand arrangement but were consistent with either (1) parallel arrangement with adjacent strands two residues out-of-register or (2) antiparallel arrangement with adjacent strand crossing between Phe-8 and Leu-9. Arrangement 1 could support the rapid fusion rate of HFPtr because of placement of the apolar N-terminal regions of all strands on the same side of the oligomer while arrangement 2 could support the assembly of multiple fusion protein trimers.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.