Evidence map›Paper›PMID 29024246›Full record

ArticleProtein science : a publication of the Protein Society2018

PixelDB: Protein-peptide complexes annotated with structural conservation of the peptide binding mode.

Vincent Frappier, Madeleine Duran, Amy E Keating

Erratum issuedAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Tertiary motifs as building blocks for the design of protein-binding peptides.Protein science : a publication of the Protein Society · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structural and computational examination of theThe Journal of biological chemistry · 2019
    Article
  15. Article
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Vincent FrappierMIT Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts.ORCID 0000-0002-4281-3128
Madeleine DuranMIT Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts.
Amy E KeatingMIT Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts.

Funding

Computationally guided design of helical peptide interaction reagentsR01GM110048 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KEATING, AMY E · 2014 to 2020
$1.8M
NIGMS NIH HHS R01 GM110048
6 · The paper itself

Abstract

PixelDB, the Peptide Exosite Location Database, compiles 1966 non-redundant, high-resolution structures of protein-peptide complexes filtered to minimize the impact of crystal packing on peptide conformation. The database is organized to facilitate study of structurally conserved versus non-conserved elements of protein-peptide engagement. PixelDB clusters complexes based on the structural similarity of the peptide-binding protein, and by comparing complexes within a cluster highlights examples of domains that engage peptides using more than one binding mode. PixelDB also identifies conserved peptide core structural motifs characteristic of each binding mode. Peptide regions that flank core motifs often make non-structurally conserved interactions with the protein surface in regions we call exosites. Many examples establish that exosite contacts can be important for enhancing protein binding and interaction specificity. PixelDB provides a resource for computational and structural biologists to study, model, and predict core-motif and exosite-contacting peptide interactions. PixelDB is available to the community without restriction in a convenient flat-file format with accompanying visualization tools.

Indexed as

Databases, ProteinModels, MolecularMultiprotein ComplexesPeptidesProteinsMultiprotein ComplexesPeptidesProteinsexositespeptide binding motifspeptide dockingprotein-peptide interactionsstructural biology database

Identifiers

PMID29024246
PMCPMC5734312

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.