Evidence map›Paper›PMID 30584092›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation.

Ivan B Lomakin, Sergey E Dmitriev, Thomas A Steitz

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Hepatitis C Virus Translation Regulation.International journal of molecular sciences · 2020
    Review
  12. A Retrospective on eIF2A-and Not the Alpha Subunit of eIF2.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Crystal structure of the C-terminal domain of DENR.Computational and structural biotechnology journal · 2020
    Article
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

3 authors.

Ivan B LomakinDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114; ivan.lomakin@yale.edu.ORCID 0000-0001-6528-5068
Sergey E DmitrievBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.
Thomas A SteitzDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114.

Funding

X-RAY ANALYSIS OF PROTEIN STRUCTURE AND FUNCTIONP01GM022778 · NIGMS · YALE UNIVERSITY · PI BREAKER, RONALD R · 1985 to 2019
$26.1M
Howard Hughes Medical InstituteNIGMS NIH HHS P01 GM022778
6 · The paper itself

Abstract

The density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein support noncanonical translation initiation, promote translation reinitiation on a specific set of mRNAs with short upstream reading frames, and regulate ribosome recycling. DENR and MCT-1 form a heterodimer, which binds to the ribosome. We determined the crystal structure of the heterodimer formed by human MCT-1 and the N-terminal domain of DENR at 2.0-Å resolution. The structure of the heterodimer reveals atomic details of the mechanism of DENR and MCT-1 interaction. Four conserved cysteine residues of DENR (C34, C37, C44, C53) form a classical tetrahedral zinc ion-binding site, which preserves the structure of the DENR's MCT-1-binding interface that is essential for the dimerization. Substitution of all four cysteines by alanine abolished a heterodimer formation. Our findings elucidate further the mechanism of regulation of DENR-MCT-1 activities in unconventional translation initiation, reinitiation, and recycling.

Indexed as

Protein MultimerizationCell Cycle ProteinsEukaryotic Initiation FactorsHumansOncogene ProteinsProtein Structure, QuaternaryCell Cycle ProteinsDENR protein, humanEukaryotic Initiation FactorsMCTS1 protein, humanOncogene Proteinsprotein synthesis regulationtranslation initiationtranslation recyclingtranslation reinitiationzinc binding

Identifiers

PMID30584092
PMCPMC6329987

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.