Evidence map›Paper›PMID 29056482›Full record

ArticleStructure (London, England : 1993)2017

Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.

R Elliot Murphy, Alexandra B Samal, Jiri Vlach, Jamil S Saad

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed.

  1. Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026
    Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Conformational Variability of HIV-1 Env Trimer and Viral Vulnerability.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

R Elliot MurphyDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Alexandra B SamalDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Jiri VlachDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Jamil S SaadDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA. Electronic address: saad@uab.edu.

Funding

XRAY CRYSTALLOGRAPHYP30CA013148 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Omer Jamy · 1985 to 2026
$165.9M
Virology CoreP30AI027767 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Paul A. Goepfert · 1988 to 2026
$84.1M
Structural Basis for HIV-1 Gag Interactions with Cellular ConstituentsR01GM117837 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SAAD, JAMIL SUBHI · 2015 to 2018
$1.7M
NCI NIH HHS P30 CA013148NIAID NIH HHS P30 AI027767NIGMS NIH HHS R01 GM117837
6 · The paper itself

Abstract

The cytoplasmic tail of gp41 (gp41CT) remains the last HIV-1 domain with an unknown structure. It plays important roles in HIV-1 replication such as mediating envelope (Env) intracellular trafficking and incorporation into assembling virions, mechanisms of which are poorly understood. Here, we present the solution structure of gp41CT in a micellar environment and characterize its interaction with the membrane. We show that the N-terminal 45 residues are unstructured and not associated with the membrane. However, the C-terminal 105 residues form three membrane-bound amphipathic α helices with distinctive structural features such as variable degree of membrane penetration, hydrophobic and basic surfaces, clusters of aromatic residues, and a network of cation-π interactions. This work fills a major gap by providing the structure of the last segment of HIV-1 Env, which will provide insights into the mechanisms of Gag-mediated Env incorporation as well as the overall Env mobility and conformation on the virion surface.

Indexed as

Amino Acid SequenceBinding SitesCloning, MolecularDimyristoylphosphatidylcholineEscherichia coliGene ExpressionGenetic VectorsHIV-1HIV Envelope Protein gp41Hydrophobic and Hydrophilic InteractionsLipid BilayersMicellesModels, MolecularNuclear Magnetic Resonance, BiomolecularPhospholipid EthersProtein Binding1,2-dihexadecyl-sn-glycero-3-phosphocholineDimyristoylphosphatidylcholinegp41 protein, Human immunodeficiency virus 1HIV Envelope Protein gp41Lipid BilayersMicellesPhospholipid EthersRecombinant Proteinsbicellescytoplasmic tailenvelope proteinGag polyproteingp41HIV-1matrix proteinmembranemicellesNMR

Identifiers

PMID29056482
PMCPMC5687296

What OpenQuestion holds

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Registered trials

None linked

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.