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A Survey of Predicted Protein-Protein Interactions Involving Disordered Regions in Humans.

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Summary

Intrinsically disordered regions (IDRs) in proteins are key to protein-protein interactions (PPIs). Our study reveals IDRs primarily bind ordered domains, with mutations in these interfaces linked to human diseases.

Keywords:
AlphaFold2human proteomeintrinsically disordered regionsprotein–protein interactionssequence conservation

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Genomics

Background:

  • Intrinsically disordered regions (IDRs) are crucial for protein-protein interactions (PPIs).
  • Understanding the role of IDRs in mediating PPIs is vital for comprehending cellular functions and disease mechanisms.

Purpose of the Study:

  • To predict and analyze PPIs involving intrinsically disordered regions across the human proteome.
  • To investigate the characteristics of disordered regions involved in PPIs and their relationship with protein structure and function.

Main Methods:

  • Utilized AlphaFold2 for PPI prediction.
  • Employed enriched multiple sequence alignments for analysis.
  • Investigated sequence conservation, domain composition, and post-translational modifications in IDRs.

Main Results:

  • Disordered regions predominantly interact with ordered domains; disordered-disordered interactions are rare.
  • Specific disordered regions (e.g., keratin type II head, KRAB) mediate interactions with diverse ordered domains (e.g., kinase, WD40).
  • Interacting disordered regions show higher sequence conservation and enrichment of disease-associated mutations and post-translational modifications.

Conclusions:

  • IDRs play a significant role in mediating PPIs, often interacting with ordered protein domains.
  • Sequence conservation and post-translational modifications highlight the functional importance and regulation of IDR-mediated interactions.
  • The enrichment of disease mutations in these interfaces underscores the pathological relevance of IDR-mediated PPIs in human health and disease.