Evidence map›Paper›PMID 23201273›Full record

ArticleStructure (London, England : 1993)2013

Nonspecific recognition is achieved in Pot1pC through the use of multiple binding modes.

Thayne H Dickey, Marissa A McKercher, Deborah S Wuttke

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A comparative study of protein-ssDNA interactions.NAR genomics and bioinformatics · 2021
    Article
  6. Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020
    Review
  7. Article
  8. Article
  9. Single-stranded telomere-binding protein employs a dual rheostat for binding affinity and specificity that drives function.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Thayne H DickeyDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Marissa A McKercherDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Deborah S WuttkeDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA. Electronic address: deborah.wuttke@colorado.edu.
University of Colorado Boulder · US

Funding

Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
SINGLE STRANDED DNA RECOGNITION IN TELOMERESR01GM059414 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI WUTTKE, DEBORAH S. · 1999 to 2015
$3.7M
Mechanistic studies of protein reorganization in a virusF32GM065013 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI LEE, KELLY K · 2002 to 2004
$125k
NIGMS NIH HHS F32 GM065013NIGMS NIH HHS GM059414NIGMS NIH HHS R01 GM059414NIGMS NIH HHS T32 GM065103NIGMS NIH HHS T32 GM65013
6 · The paper itself

Abstract

Pot1 is the protein responsible for binding to and protecting the 3' single-stranded DNA (ssDNA) overhang at most eukaryotic telomeres. Here, we present the crystal structure of one of the two oligonucleotide/oligosaccharide-binding folds (Pot1pC) that make up the ssDNA-binding domain in S. pombe Pot1. Comparison with the homologous human domain reveals unexpected structural divergence in the mode of ligand binding that explains the differing ligand requirements between species. Despite the presence of apparently base-specific hydrogen bonds, Pot1pC is able to bind a wide range of ssDNA sequences with thermodynamic equivalence. To address how Pot1pC binds ssDNA with little to no specificity, multiple structures of Pot1pC bound to noncognate ssDNA ligands were solved. These structures reveal that this promiscuity is implemented through new binding modes that thermodynamically compensate for base-substitutions through alternate stacking interactions and new H-bonding networks.

Indexed as

SchizosaccharomycesBinding SitesCrystallography, X-RayDNA, FungalDNA, Single-StrandedHydrogen BondingModels, MolecularNucleic Acid ConformationProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySchizosaccharomyces pombe ProteinsShelterin ComplexTelomere-Binding ProteinsDNA, FungalDNA, Single-Strandedpot1 protein, S pombeSchizosaccharomyces pombe ProteinsShelterin ComplexTelomere-Binding Proteins

Identifiers

PMID23201273
PMCPMC3545015
OpenAlexW2100826791

What OpenQuestion holds

Textmetadata
LicenceTDM
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.