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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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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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Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Pathogenic variations illuminate functional constraints in intrinsically disordered proteins.

Norbert Deutsch1, Gábor Erdős1, Zsuzsanna Dosztányi1

  • 1Department of Biochemistry, Eötvös Loránd University, Pázmány Péter Stny 1/c, 1117 Budapest, Hungary.

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Intrinsically disordered regions (IDRs) are crucial for cell regulation but their disease links are unclear. This study identifies pathogenic variants within IDRs, revealing new insights into genetic disease mechanisms.

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Area of Science:

  • Genomics
  • Molecular Biology
  • Bioinformatics

Background:

  • Intrinsically disordered regions (IDRs) are vital for cellular signaling and regulation.
  • The role of IDRs in human disease is not well understood.
  • Missense variants in IDRs may contribute to disease pathogenesis.

Purpose of the Study:

  • To investigate the contribution of intrinsically disordered regions to human disease.
  • To analyze the distribution and impact of missense variants within IDRs.
  • To develop a framework for interpreting variants of uncertain significance in IDRs.

Main Methods:

  • Analysis of nearly one million ClinVar missense variants within IDRs.
  • Application of AlphaMissense for predicting pathogenicity.
  • Development of a classifier to prioritize predicted ELM motifs (PEMs).

Main Results:

  • Pathogenic variants are enriched in short linear motifs (SLiMs) and disordered binding regions within IDRs.
  • AlphaMissense identified localized "island-like" patterns of elevated pathogenicity in IDRs.
  • Thousands of candidate functional sites linked to neurological, cardiovascular, and cancer diseases were revealed.

Conclusions:

  • Genetic variation within IDRs significantly contributes to human disease.
  • This framework offers a scalable strategy for interpreting variants of uncertain significance.
  • Understanding functional constraints in the disordered proteome is crucial for disease research.