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CRTAC1 has a Compact β-propeller-TTR Core Stabilized by Potassium Ions.

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Summary
This summary is machine-generated.

Potassium ions stabilize Cartilage acidic protein-1 (CRTAC1), a protein involved in nervous system repair and disease. This study reveals CRTAC1

Keywords:
LOTUScartilage acidic protein-1crystal structurepotassium bindingprotein stabilization

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Cartilage acidic protein-1 (CRTAC1) is a secreted glycoprotein implicated in nervous system development, repair, and various diseases, including stroke, osteoarthritis, and cancer.
  • Previous structural characterization of CRTAC1 was hindered by its propensity to form disulfide-linked aggregates.

Purpose of the Study:

  • To elucidate the structure of CRTAC1 and understand the factors contributing to its stability.
  • To investigate the role of potassium ions in CRTAC1 structure and aggregation.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structure of CRTAC1.
  • Analysis of bound ions and site-directed mutagenesis of cysteine residues were performed.
  • Investigated the impact of potassium ion concentration on protein stability and aggregation.

Main Results:

  • The study determined the 1.6 Å resolution structure of CRTAC1, revealing a novel three-domain fold comprising a β-propeller-TTR combination.
  • Ten ions were observed bound to CRTAC1: six calcium, three potassium, and one sodium.
  • Potassium ions are crucial for CRTAC1 stability, with binding sites located between β-propeller blades, and their absence exposes buried cysteines, facilitating aggregation.

Conclusions:

  • Potassium ions stabilize the CRTAC1 structure by binding within the β-propeller domain, preventing aggregation.
  • The identified potassium binding sites are structurally conserved within the CRTAC protein family.
  • These findings provide a foundation for understanding CRTAC1's function in health and disease.