Evidence map›Paper›PMID 27242869›Full record

ArticleFrontiers in plant science2016

Crystal Structure of Hyp-1, a Hypericum perforatum PR-10 Protein, in Complex with Melatonin.

Joanna Sliwiak, Zbigniew Dauter, Mariusz Jaskolski

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2016. 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
2.7field-weighted citation impact, top 10% of its field
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, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Diverse Therapeutic Potentials of Hypericin: An In-Depth Review.Current topics in medicinal chemistry · 2025
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Melatonin Target Proteins: Too Many or Not Enough?Frontiers in endocrinology · 2019
    Review
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 at 3 institutions in 2 countries.

Joanna SliwiakCenter for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences Poznan, Poland.
Zbigniew DauterSynchrotron Radiation Research Section, National Cancer Institute, Argonne National Laboratory, Argonne IL, USA.
Mariusz JaskolskiCenter for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of SciencesPoznan, Poland; Department of Crystallography, Faculty of Chemistry, Adam Mickiewicz University in PoznańPoznań, Poland.
Adam Mickiewicz University in Poznań · PLArgonne National Laboratory · USInstitute of Bioorganic Chemistry, Polish Academy of Sciences · PL

Funding

Macromolecular Crystallography Research with Synchrotron RadiationZIABC010378 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DAUTER, ZBIGNIEW · 2009 to 2020
$18.8M
6 · The paper itself

Abstract

Hyp-1, a PR-10-fold protein from Hypericum perforatum, was crystallized in complex with melatonin (MEL). The structure confirms the conserved protein fold and the presence of three unusual ligand binding sites, two of which are internal chambers (1,2), while the third one (3) is formed as an invagination of the protein surface. The MEL ligand in site 1 is well defined while that in site 3 seems to be rotating between the side chains of Lys33 and Tyr150 that act as a molecular vise. The patch of electron density in site 2 does not allow unambiguous modeling of a melatonin molecule but suggests a possible presence of its degradation product. This pattern of ligand occupation is reproducible in repeated crystallization/structure determination experiments. Although the binding of melatonin by Hyp-1 does not appear to be very strong (for example, MEL cannot displace the artificial fluorescence probe ANS), it is strong enough to suggest a physiological role of this interaction. For example, trans-zeatin, which is a common ligand of PR-10 proteins, does not overcompete melatonin for binding to Hyp-1 as it does not affect the crystallization process of the Hyp-1/MEL complex, and among a number of potential natural mediators tested, melatonin was the only one to form a crystalline complex with Hyp-1 with the use of standard crystallization screens. Hyp-1 is the second protein in the Protein Data Bank for which melatonin binding has been demonstrated crystallographically, the first one being human quinone reductase.

Indexed as

cytokininligand bindingpathogenesis-related proteinphytohormonePR-10

Identifiers

PMID27242869
PMCPMC4870859
OpenAlexW2408112837

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.