Evidence map›Paper›PMID 40433978›Full record

ArticleNucleic acids research2025

Structural basis of G-quadruplex recognition by a camelid antibody fragment.

Mojca Pevec, Tadej Medved, Matic Kovačič, Neža Žerjav, Jernej Imperl, Janez Plavec, Jurij Lah, Remy Loris, San Hadži

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. AVIDbase: A biologically accurate structural dataset of nanobody-antigen complexes.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. 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

9 authors.

Mojca PevecDepartment of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.ORCID 0000-0001-5968-3895
Tadej MedvedDepartment of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.
Matic KovačičSlovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Neža ŽerjavDepartment of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.
Jernej ImperlDepartment of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.
Janez PlavecSlovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0003-1570-8602
Jurij LahDepartment of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.ORCID 0000-0003-1021-3803
Remy LorisStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.ORCID 0000-0002-8862-3338
San HadžiDepartment of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.ORCID 0000-0002-5615-7918

Funding

Eutopia Foundation G003320NSlovenian Research and Innovation Agency J1-50026Slovenian Research and Innovation Agency P1-0201Slovenian Research and Innovation Agency P1-0242
6 · The paper itself

Abstract

Apart from the iconic Watson-Crick duplex, DNA can fold into different noncanonical structures, of which the most studied are G-quadruplexes (G4s). Despite mounting structural and biophysical evidence, their existence in cells was controversial until their detection using G4-specific antibodies. However, it remains unknown how antibodies recognize G4s at the molecular level and why G4-specific antibodies have low selectivity and are unable to distinguish different G4 sequences. Here, we present the crystal structure of a nanobody bound to the archetypical G4 structure, the thrombin-binding aptamer (TBA). The nanobody exhibits strong selectivity against different G4 sequences and utilizes an unusual scaffold-based paratope, with very limited involvement of complementarity-determining region. The nanobody effectively mimics the binding interface of thrombin, a natural binding partner of TBA, by using isosteric interactions at key positions. The presented structure sheds light on the molecular basis of how antibodies, essential G4-detection tools, recognize noncanonical G4 structures.

Indexed as

Aptamers, NucleotideG-QuadruplexesSingle-Domain AntibodiesAnimalsBinding SitesComplementarity Determining RegionsCrystallography, X-RayDNAHumansModels, MolecularProtein BindingThrombinAptamers, NucleotideComplementarity Determining RegionsDNASingle-Domain AntibodiesThrombinthrombin aptamer

Identifiers

PMID40433978
PMCPMC12117401

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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.