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Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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DisProt in 2024: improving function annotation of intrinsically disordered proteins.

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Summary

DisProt, a key database for intrinsically disordered proteins, now offers enhanced functional annotations and improved data quality. This update increases coverage and provides insights into protein structures, aiding research in molecular biology.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs) play crucial roles in cellular functions but lack stable structures.
  • DisProt is a leading database for experimentally verified IDPs and intrinsically disordered regions (IDRs).

Purpose of the Study:

  • To present the latest advancements in the DisProt database, focusing on enhanced functional annotations and curation.
  • To improve the quality and sequence-level coverage of annotations for IDPs and IDRs.
  • To explore the correlation between curated disorder data and structure prediction confidence scores.

Main Methods:

  • Systematic application of Minimum Information About Disorder Experiments (MIADE) principles for improved annotation quality.
  • Expansion of Gene Ontology (GO) term usage for a broader functional repertoire.
  • Adoption of additional evidence codes to increase annotation coverage.
  • Comparison of DisProt annotations with AlphaFold2 predicted Local Distance Difference Test (pLDDT) confidence scores.

Main Results:

  • Significant improvements in annotation quality and sequence coverage for intrinsically disordered proteins and regions.
  • Expanded functional repertoire through new thematic datasets and increased GO term adoption, automatically propagated to UniProtKB.
  • Strong correlation observed between DisProt's curated annotations and AlphaFold2 pLDDT scores, validating experimental data and aiding interpretation of predicted structures.

Conclusions:

  • The updated DisProt database serves as a comprehensive resource for intrinsically disordered proteins, integrating experimental evidence.
  • Enhanced annotations and coverage provide deeper insights into the functions and structural characteristics of IDPs.
  • DisProt aids in understanding complex protein structures, particularly folding-upon-binding fragments, by correlating experimental data with computational predictions.