Evidence map›Paper›PMID 28874805›Full record

ArticleScientific reports2017

Modular assembly of a protein nanotriangle using orthogonally interacting coiled coils.

Won Min Park, Mostafa Bedewy, Karl K Berggren, Amy E Keating

Abstract read
In one paragraph

Article in Scientific reports, 2017. 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. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Crystal Structure ofJournal of the American Chemical Society · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Docking domain-mediated subunit interactions in natural product megasynth(et)ases.Journal of industrial microbiology & biotechnology · 2021
    Review
  11. A nanobody toolbox targeting dimeric coiled-coil modules for functionalization of designed protein origami structures.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. TriangularACS chemical biology · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Quarterly reviews of biophysics · 2020
    Review
  17. Synthetic Control of Tertiary Helical Structures in Short Peptides.Journal of the American Chemical Society · 2018
    Article
  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

4 authors.

Won Min ParkDepartment of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, 02139, USA.
Mostafa BedewyResearch Laboratory of Electronics, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, 02139, USA.ORCID 0000-0003-4182-7533
Karl K BerggrenResearch Laboratory of Electronics, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, 02139, USA.
Amy E KeatingDepartment of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, 02139, USA. keating@mit.edu.

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

Synthetic protein assemblies that adopt programmed shapes would support many applications in nanotechnology. We used a rational design approach that exploits the modularity of orthogonally interacting coiled coils to create a self-assembled protein nanotriangle. Coiled coils have frequently been used to construct nanoassemblies and materials, but rarely with successful prior specification of the resulting structure. We designed a heterotrimer from three pairs of heterodimeric coiled coils that mediate specific interactions while avoiding undesired crosstalk. Non-associating pairs of coiled-coil units were strategically fused to generate three chains that were predicted to preferentially form the heterotrimer, and a rational annealing process led to the desired oligomer. Extensive biophysical characterization and modeling support the formation of a molecular triangle, which is a shape distinct from naturally occurring supramolecular nanostructures. Our approach can be extended to design more complex nanostructures using additional coiled-coil modules, other protein parts, or templated surfaces.

Indexed as

Models, MolecularProtein ConformationMicroscopy, Atomic ForceProtein FoldingProtein MultimerizationProteinsThermodynamicsProteins

Identifiers

PMID28874805
PMCPMC5585338

What OpenQuestion holds

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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.