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Investigating protein aggregation in protein-carbohydrate interfaces using sequence and structural features.

S Lekshmi1, N R Siva Shanmugam2, R Prabakaran3

  • 1Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology, Chennai 600036, India.

Biochimica Et Biophysica Acta. Proteins and Proteomics
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Summary
This summary is machine-generated.

Aggregation-prone regions (APRs) in proteins can bind carbohydrates, challenging assumptions about their role in cellular processes. These functional APRs (fAPRs) are important sites for mutations linked to disease.

Keywords:
Aggregating peptidesAggregation-prone regionsCarbohydrate-binding proteinsProtein aggregationProtein-carbohydrate interactions

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein-carbohydrate interactions are vital for cellular functions like signaling and immunity.
  • Aggregation-prone regions (APRs) are typically linked to protein misfolding and disease.
  • Previous studies suggest some aggregating peptides bind carbohydrates, prompting investigation into APRs in protein-carbohydrate complexes.

Purpose of the Study:

  • To systematically analyze aggregation-prone regions (APRs) in protein-carbohydrate complexes.
  • To determine if APRs correspond to carbohydrate-binding residues at sequence and structural levels.
  • To investigate the functional implications and mutation landscape of APRs at carbohydrate-binding sites.

Main Methods:

  • Analysis of curated protein-carbohydrate complexes.
  • Examination of APRs at protein sequence and structural levels.
  • Identification and characterization of functional APRs (fAPRs).

Main Results:

  • Carbohydrate-binding proteins show enrichment of APRs; 40% of carbohydrate-binding residues are aggregation-prone.
  • Functional APRs (fAPRs) are enriched with aromatic residues that facilitate carbohydrate binding.
  • Aggregation propensity and carbohydrate-binding affinity are independently modulated at fAPRs.
  • 85% of human fAPRs contain mutations predicted as 'likely pathogenic'.

Conclusions:

  • APRs can be functionally integrated into carbohydrate-binding sites, contrary to their association with proteostasis disruption.
  • Functional APRs (fAPRs) represent critical sites where aggregation and carbohydrate binding intersect.
  • fAPRs are hotspots for disease-associated mutations, offering insights into mutation effects.