Evidence map›Paper›PMID 26683124›Full record

ArticleProtein science : a publication of the Protein Society2016

Resolving the ambiguity: Making sense of intrinsic disorder when PDB structures disagree.

Shelly DeForte, Vladimir N Uversky

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026
    Article
  2. I-Shaped Dimers of a Plant Chloroplast FInternational journal of molecular sciences · 2023
    Article
  3. Review
  4. Review
  5. ATP synthase FCellular and molecular life sciences : CMLS · 2022
    Review
  6. Article
  7. Review
  8. Diffusion of a disordered protein on its folded ligand.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Homology modeling in the time of collective and artificial intelligence.Computational and structural biotechnology journal · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Dissecting physical structure of calreticulin, an intrinsically disordered CaJournal of biomolecular structure & dynamics · 2018
    Article
  20. Review
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

Shelly DeForteDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, Florida, 33612.
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, Florida, 33612.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Missing regions in X-ray crystal structures in the Protein Data Bank (PDB) have played a foundational role in the study of intrinsically disordered protein regions (IDPRs), especially in the development of in silico predictors of intrinsic disorder. However, a missing region is only a weak indication of intrinsic disorder, and this uncertainty is compounded by the presence of ambiguous regions, where more than one structure of the same protein sequence "disagrees" in terms of the presence or absence of missing residues. The question is this: are these ambiguous regions intrinsically disordered, or are they the result of static disorder that arises from experimental conditions, ensembles of structures, or domain wobbling? A novel way of looking at ambiguous regions in terms of the pattern between multiple PDB structures has been demonstrated. It was found that the propensity for intrinsic disorder increases as the level of ambiguity decreases. However, it is also shown that ambiguity is more likely to occur as the protein region is placed within different environmental conditions, and even the most ambiguous regions as a set display compositional bias that suggests flexibility. The results suggested that ambiguity is a natural result for many IDPRs crystallized under different conditions and that static disorder and wobbling domains are relatively rare. Instead, it is more likely that ambiguity arises because many of these regions were conditionally or partially disordered.

Indexed as

Amino Acid SequenceCrystallography, X-RayDatabases, ProteinIntrinsically Disordered ProteinsProtein ConformationProtein Structure, SecondaryIntrinsically Disordered Proteinsdisorder predictionintrinsically disordered proteinintrinsically disordered protein regionmissing residuesPDBprotein data bankX-ray crystallography

Identifiers

PMID26683124
PMCPMC4815412

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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.