Evidence map›Paper›PMID 22927388›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Foldon unfolding mediates the interconversion between M(pro)-C monomer and 3D domain-swapped dimer.

Xue Kang, Nan Zhong, Peng Zou, Shengnan Zhang, Changwen Jin, Bin Xia

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. SARS-CoV-2 MACS central science · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Domain-swapped cytochromeChemical science · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Evidences for the unfolding mechanism of three-dimensional domain swapping.Protein science : a publication of the Protein Society · 2013
    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

6 authors.

Xue KangBeijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, China.
Nan Zhong
Peng Zou
Shengnan Zhang
Changwen Jin
Bin Xia

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-terminal domain (M(pro)-C) of SARS-CoV main protease adopts two different fold topologies, a monomer and a 3D domain-swapped dimer. Here, we report that M(pro)-C can reversibly interconvert between these two topological states under physiological conditions. Although the swapped α(1)-helix is fully buried inside the protein hydrophobic core, the interconversion of M(pro)-C is carried out without the hydrophobic core being exposed to solvent. The 3D domain swapping of M(pro)-C is activated by an order-to-disorder transition of its C-terminal α(5)-helix foldon. Unfolding of this foldon promotes self-association of M(pro)-C monomers and functions to mediate the 3D domain swapping, without which M(pro)-C can no longer form the domain-swapped dimer. Taken together, we propose that there exists a special dimeric intermediate enabling the protein core to unpack and the α(1)-helices to swap in a hydrophobic environment, which minimizes the energy cost of the 3D domain-swapping process.

Indexed as

Protein ConformationProtein FoldingCircular DichroismCoronavirus 3C ProteasesCysteine EndopeptidasesDimerizationKineticsMagnetic Resonance SpectroscopyMutagenesisMutationSpin LabelsThermodynamicsViral ProteinsCoronavirus 3C ProteasesCysteine EndopeptidasesSpin LabelsViral Proteins

Identifiers

PMID22927388
PMCPMC3443179

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.