Evidence map›Paper›PMID 24550273›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

Jacint G Sanchez, Katarzyna Okreglicka, Viswanathan Chandrasekaran, Jordan M Welker, Wesley I Sundquist, Owen Pornillos

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing 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

123 citing papers in PubMed.

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  16. Review
  17. Article
  18. Review
  19. Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025
    Review
  20. A minimal complex of KHNYN and zinc-finger antiviral protein binds and degrades single-stranded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

63 more citing papers are in PubMed but not listed here.

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

6 authors.

Jacint G SanchezDepartment of Molecular Physiology and Biological Physics and The Myles H. Thaler Center for AIDS and Human Retrovirus Research, University of Virginia, Charlottesville, VA 22908.
Katarzyna Okreglicka
Viswanathan Chandrasekaran
Jordan M Welker
Wesley I Sundquist
Owen Pornillos

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
TRAINING IN CELL AND MOLECULAR BIOLOGYT32GM008136 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI STUKENBERG, P. TODD · 1985 to 2020
$8.5M
Structural Virology of Tripartite Motif ProteinsR01GM112508 · NIGMS · UNIVERSITY OF VIRGINIA · PI PORNILLOS, OWEN · 2014 to 2018
$1.6M
NIGMS NIH HHS P50 GM082545NIGMS NIH HHS R01 GM112508NIGMS NIH HHS T32 GM008136
6 · The paper itself

Abstract

Tripartite motif (TRIM) proteins make up a large family of coiled-coil-containing RING E3 ligases that function in many cellular processes, particularly innate antiviral response pathways. Both dimerization and higher-order assembly are important elements of TRIM protein function, but the atomic details of TRIM tertiary and quaternary structure have not been fully understood. Here, we present crystallographic and biochemical analyses of the TRIM coiled-coil and show that TRIM proteins dimerize by forming interdigitating antiparallel helical hairpins that position the N-terminal catalytic RING domains at opposite ends of the dimer and the C-terminal substrate-binding domains at the center. The dimer core comprises an antiparallel coiled-coil with a distinctive, symmetric pattern of flanking heptad and central hendecad repeats that appear to be conserved across the entire TRIM family. Our studies reveal how the coiled-coil organizes TRIM25 to polyubiquitylate the RIG-I/viral RNA recognition complex and how dimers of the TRIM5α protein are arranged within hexagonal arrays that recognize the HIV-1 capsid lattice and restrict retroviral replication.

Indexed as

Evolution, MolecularModels, MolecularProtein ConformationBase SequenceCrystallography, X-RayDimerizationFluorometryHumansMolecular Sequence DataProtein Structure, TertiaryRosaniline DyesSequence Analysis, DNATranscription FactorsTripartite Motif ProteinsUbiquitin-Protein LigasesUltracentrifugationCoomassie blueRosaniline DyesTranscription FactorsTRIM25 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligasesantiparallel dimerdisulfide crosslinkingX-ray crystallography

Identifiers

PMID24550273
PMCPMC3932864

What OpenQuestion holds

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Registered trials

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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.