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Human CCL5 trimer: expression, purification and initial crystallographic studies.

Yi Chen Chen1, Kun Mou Li1, Raz Zarivach2

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Acta Crystallographica. Section F, Structural Biology Communications
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Summary
This summary is machine-generated.

Chemokine CCL5

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RANTESchemokineshuman CCL5 trimer

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Area of Science:

  • Structural Biology
  • Immunology
  • Biochemistry

Background:

  • Chemokine CCL5 recruits immune cells to inflammatory sites, playing a role in immune responses.
  • CCL5 oligomerization is crucial for cell migration, immune activation, and HIV entry, but its structure and formation mechanism remain unclear.

Purpose of the Study:

  • To elucidate the structure of high-order CCL5 oligomers.
  • To understand the mechanism of CCL5 oligomerization.

Main Methods:

  • A CCL5 mutant (CCL5-E66S) deficient in oligomerization was combined with native CCL5 to form trimers.
  • Trimeric CCL5 was crystallized under optimized conditions.
  • X-ray diffraction data were collected to a resolution of 1.87 Å.

Main Results:

  • Trimeric CCL5 crystallized in the tetragonal space group P4₁2₁2.
  • The crystal structure revealed interfaces within the CCL5 oligomer.
  • Diffraction data quality was satisfactory, with a resolution of 1.87 Å.

Conclusions:

  • The determined structure provides insights into the interfaces of CCL5 oligomers.
  • This structural information aids in understanding the mechanism of CCL5 oligomerization.
  • The findings may inform the development of therapeutic strategies targeting CCL5.