Evidence map›Paper›PMID 19333395›Full record

ArticlePloS one2009

Length variations amongst protein domain superfamilies and consequences on structure and function.

Sankaran Sandhya, Saane Sudha Rani, Barah Pankaj, Madabosse Kande Govind, Bernard Offmann, Narayanaswamy Srinivasan, Ramanathan Sowdhamini

Abstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

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0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Diversity in protein domain superfamilies.Current opinion in genetics & development · 2015
    Review
  16. The Recent De Novo Origin of Protein C-Termini.Genome biology and evolution · 2015
    Article
  17. Article
  18. Article
  19. Use of a structural alphabet to find compatible folds for amino acid sequences.Protein science : a publication of the Protein Society · 2015
    Article
  20. Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Sankaran SandhyaNational Centre for Biological Sciences (TIFR), GKVK Campus, Bangalore, India.
Saane Sudha Rani
Barah Pankaj
Madabosse Kande Govind
Bernard Offmann
Narayanaswamy Srinivasan
Ramanathan Sowdhamini

Funding

Wellcome Trust
6 · The paper itself

Abstract

backgroundRelated protein domains of a superfamily can be specified by proteins of diverse lengths. The structural and functional implications of indels in a domain scaffold have been examined. METHODOLOGY: In this study, domain superfamilies with large length variations (more than 30% difference from average domain size, referred as 'length-deviant' superfamilies and 'length-rigid' domain superfamilies (<10% length difference from average domain size) were analyzed for the functional impact of such structural differences. Our delineated dataset, derived from an objective algorithm, enables us to address indel roles in the presence of peculiar structural repeats, functional variation, protein-protein interactions and to examine 'domain contexts' of proteins tolerant to large length variations. Amongst the top-10 length-deviant superfamilies analyzed, we found that 80% of length-deviant superfamilies possess distant internal structural repeats and nearly half of them acquired diverse biological functions. In general, length-deviant superfamilies have higher chance, than length-rigid superfamilies, to be engaged in internal structural repeats. We also found that approximately 40% of length-deviant domains exist as multi-domain proteins involving interactions with domains from the same or other superfamilies. Indels, in diverse domain superfamilies, were found to participate in the accretion of structural and functional features amongst related domains. With specific examples, we discuss how indels are involved directly or indirectly in the generation of oligomerization interfaces, introduction of substrate specificity, regulation of protein function and stability.

conclusionsOur data suggests a multitude of roles for indels that are specialized for domain members of different domain superfamilies. These specialist roles that we observe and trends in the extent of length variation could influence decision making in modeling of new superfamily members. Likewise, the observed limits of length variation, specific for each domain superfamily would be particularly relevant in the choice of alignment length search filters commonly applied in protein sequence analysis.

Indexed as

Amino Acid SequenceDatabases, ProteinProtein Interaction MappingProteinsProtein Structure, TertiaryProteomicsProteins

Identifiers

PMID19333395
PMCPMC2659687

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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.