Evidence map›Paper›PMID 23946125›Full record

ArticleProteins2013

Global and local structural similarity in protein-protein complexes: implications for template-based docking.

Petras J Kundrotas, Ilya A Vakser

Abstract read
In one paragraph

Article in Proteins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. Toward Characterising the Cellular 3D-Proteome.Frontiers in bioinformatics · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Dockground: A comprehensive data resource for modeling of protein complexes.Protein science : a publication of the Protein Society · 2018
    Article
  8. Article
  9. Article
  10. HOMCOS: an updated server to search and model complex 3D structures.Journal of structural and functional genomics · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Template-based structure modeling of protein-protein interactions.Current opinion in structural biology · 2014
    Review
  18. 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

2 authors.

Petras J KundrotasCenter for Bioinformatics, The University of Kansas, Lawrence, Kansas.
Ilya A Vakser

Funding

Integrated Resource for Protein Recognition StudiesR01GM074255 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI VAKSER, ILYA · 2005 to 2024
$6.2M
NIGMS NIH HHS R01 GM074255
6 · The paper itself

Abstract

The increasing amount of structural information on protein-protein interactions makes it possible to predict the structure of protein-protein complexes by comparison/alignment of the interacting proteins to the ones in cocrystallized complexes. In the predictions based on structure similarity, the template search is performed by structural alignment of the target interactors with the entire structures or with the interface only of the subunits in cocrystallized complexes. This study investigates the scope of the structural similarity that facilitates the detection of a broad range of templates significantly divergent from the targets. The analysis of the target-template similarity is based on models of protein-protein complexes in a large representative set of heterodimers. The similarity of the biological and crystal packing interfaces, dissimilar interface structural motifs in overall similar structures, interface similarity to the full structure, and local similarity away from the interface were analyzed. The structural similarity at the protein-protein interfaces only was observed in ~25% of target-template pairs with sequence identity <20% and primarily homodimeric templates. For ~50% of the target-template pairs, the similarity at the interface was accompanied by the similarity of the whole structure. However, the structural similarity at the interfaces was still stronger than that of the noninterface parts. The study provides insights into structural and functional diversity of protein-protein complexes, and relative performance of the interface and full structure alignment in docking.

Indexed as

Models, MolecularMolecular Docking SimulationProtein Interaction MapsBinding SitesComputational BiologyDatabases, ProteinProtein BindingProteinsProtein Structure, TertiarySequence AlignmentSoftwareProteinsbioinformaticsprotein modelingprotein recognitionstructural templatesstructure prediction

Identifiers

PMID23946125
PMCPMC4961257

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.