Evidence map›Paper›PMID 19765314›Full record

ArticleBMC structural biology2009

Exploring protein structural dissimilarity to facilitate structure classification.

Pooja Jain, Jonathan D Hirst

Abstract read
In one paragraph

Article in BMC structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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

2 citing papers in PubMed.

  1. Article
  2. Homology-based identification and structural analysis ofComputational and structural biotechnology journal · 2024
    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.

Pooja JainSchool of Chemistry, The University of Nottingham, University Park, Nottingham NG7 2RD, UK. pcxpj1@nottingham.ac.uk
Jonathan D Hirst

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundClassification of newly resolved protein structures is important in understanding their architectural, evolutionary and functional relatedness to known protein structures. Among various efforts to improve the database of Structural Classification of Proteins (SCOP), automation has received particular attention. Herein, we predict the deepest SCOP structural level that an unclassified protein shares with classified proteins with an equal number of secondary structure elements (SSEs).

resultsWe compute a coefficient of dissimilarity (Omega) between proteins, based on structural and sequence-based descriptors characterising the respective constituent SSEs. For a set of 1,661 pairs of proteins with sequence identity up to 35%, the performance of Omega in predicting shared Class, Fold and Super-family levels is comparable to that of DaliLite Z score and shows a greater than four-fold increase in the true positive rate (TPR) for proteins sharing the Family level. On a larger set of 600 domains representing 200 families, the performance of Z score improves in predicting a shared Family, but still only achieves about half of the TPR of Omega. The TPR for structures sharing a Super-family is lower than in the first dataset, but Omega performs slightly better than Z score. Overall, the sensitivity of Omega in predicting common Fold level is higher than that of the DaliLite Z score.

conclusionClassification to a deeper level in the hierarchy is specific and difficult. So the efficiency of Omega may be attractive to the curators and the end-users of SCOP. We suggest Omega may be a better measure for structure classification than the DaliLite Z score, with the caveat that currently we are restricted to comparing structures with equal number of SSEs.

Indexed as

Databases, ProteinProtein FoldingProteinsProtein Structure, TertiaryProteins

Identifiers

PMID19765314
PMCPMC2754988

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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.