Evidence map›Paper›PMID 22959972›Full record

ArticleJournal of molecular biology2012

Crystal structure of the N-terminal domain of Nup358/RanBP2.

Susanne A Kassube, Tobias Stuwe, Daniel H Lin, C Danielle Antonuk, Johanna Napetschnig, Günter Blobel, André Hoelz

Abstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. The Molecular Architecture of the Nuclear Basket.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review
  14. Review
  15. Evolutionary divergence of the nuclear pore complex from fungi to metazoans.Protein science : a publication of the Protein Society · 2019
    Article
  16. Article
  17. Review
  18. Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1 • Nup98).Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Article
  20. Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

7 authors.

Susanne A KassubeLaboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
Tobias Stuwe
Daniel H Lin
C Danielle Antonuk
Johanna Napetschnig
Günter Blobel
André Hoelz

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
Molecular Basis of mRNA ExportR01GM117360 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Andre Hoelz · 2016 to 2026
$2.6M
NIGMS NIH HHS R01 GM117360NIGMS NIH HHS T32 GM007616
6 · The paper itself

Abstract

Key steps in mRNA export are the nuclear assembly of messenger ribonucleoprotein particles (mRNPs), the translocation of mRNPs through the nuclear pore complex (NPC), and the mRNP remodeling events at the cytoplasmic side of the NPC. Nup358/RanBP2 is a constituent of the cytoplasmic filaments of the NPC specific to higher eukaryotes and provides a multitude of binding sites for the nucleocytoplasmic transport machinery. Here, we present the crystal structure of the Nup358 N-terminal domain (NTD) at 0.95Å resolution. The structure reveals an α-helical domain that harbors three central tetratricopeptide repeats (TPRs), flanked on each side by an additional solvating amphipathic α helix. Overall, the NTD adopts an unusual extended conformation that lacks the characteristic peptide-binding groove observed in canonical TPR domains. Strikingly, the vast majority of the NTD surface exhibits an evolutionarily conserved, positive electrostatic potential, and we demonstrate that the NTD possesses the capability to bind single-stranded RNA in solution. Together, these data suggest that the NTD contributes to mRNP remodeling events at the cytoplasmic face of the NPC.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayHumansModels, MolecularMolecular ChaperonesMolecular Sequence DataNuclear Pore Complex ProteinsProtein BindingProtein ConformationRNASequence Homology, Amino AcidMolecular ChaperonesNuclear Pore Complex Proteinsran-binding protein 2RNA

Identifiers

PMID22959972
PMCPMC4226657

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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.