Evidence map›Paper›PMID 16510427›Full record

ArticleRNA (New York, N.Y.)2006

Solution structure of an informationally complex high-affinity RNA aptamer to GTP.

James M Carothers, Jonathan H Davis, James J Chou, Jack W Szostak

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Single-round deoxyribozyme discovery.Nucleic acids research · 2021
    Article
  6. Article
  7. Inside the Black Box: What Makes SELEX Better?Molecules (Basel, Switzerland) · 2019
    Review
  8. Review
  9. Article
  10. Amplification of RNA by an RNA polymerase ribozyme.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Review
  12. Article
  13. Article
  14. Comprehensive experimental fitness landscape and evolutionary network for small RNA.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

4 authors at 3 institutions in 1 country.

James M CarothersDepartment of Molecular Biology and Center for Computational and Integrative Biology, Simches Research Center 7215, Massachusetts General Hospital, 185 Cambridge Street, Boston, Massachusetts 02114, USA.
Jonathan H Davis
James J Chou
Jack W Szostak
Massachusetts General Hospital · USHarvard University · USQB3 · US

Funding

IN VITRO SELECTION AND EVOLUTION OF NEW RIBOZYMESR01GM053936 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI SZOSTAK, JACK W · 1996 to 2003
$864k
SOLUTION STRUCTURE AND MECHANISM OF A RIBOZYMEF32GM017438 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI DAVIS, JONATHAN H · 1997 to 1998
–
NIGMS NIH HHS F32 GM017438NIGMS NIH HHS GM17438NIGMS NIH HHS GM53936NIGMS NIH HHS R01 GM053936
6 · The paper itself

Abstract

Higher-affinity RNA aptamers to GTP are more informationally complex than lower-affinity aptamers. Analog binding studies have shown that the additional information needed to improve affinity does not specify more interactions with the ligand. In light of those observations, we would like to understand the structural characteristics that enable complex aptamers to bind their ligands with higher affinity. Here we present the solution structure of the 41-nt Class I GTP aptamer (K(d) = 75 nM) as determined by NMR. The backbone of the aptamer forms a reverse-S that shapes the binding pocket. The ligand nucleobase stacks between purine platforms and makes hydrogen bonds with the edge of another base. Interestingly, the local modes of interaction for the Class I aptamer and an RNA aptamer that binds ATP with a K(d) of 6 microM are very much alike. The aptamers exhibit nearly identical levels of binding specificity and fraction of ligand sequestered from the solvent (81%-85%). However, the GTP aptamer is more informationally complex (approximately 45 vs. 35 bits) and has a larger recognition bulge (15 vs. 12 nucleotides) with many more stabilizing base-base interactions. Because the aptamers have similar modes of ligand binding, we conclude that the stabilizing structural elements in the Class I aptamer are responsible for much of the difference in K(d). These results are consistent with the hypothesis that increasing the number of intra-RNA interactions, rather than adding specific contacts to the ligand, is the simplest way to improve binding affinity.

Indexed as

Aptamers, NucleotideBase SequenceGuanosine TriphosphateNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationRNAAptamers, NucleotideGuanosine TriphosphateRNA

Identifiers

PMID16510427
PMCPMC1421093
OpenAlexW2162296614

What OpenQuestion holds

Textmetadata
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.