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Related Experiment Videos

Trimeric C-type lectin domains in host defence

H J Hoppe1, K B Reid

  • 1Department of Biochemistry, University of Oxford, UK.

Structure (London, England : 1993)
|December 15, 1994
PubMed
Summary
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Crystal structures reveal that the triple-stranded alpha-helical coiled coil in mannose-binding proteins dictates the trimeric orientation of C-type lectin domains, crucial for protein function.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Mannose-binding proteins (MBPs) are collectins involved in innate immunity.
  • C-type lectin domains are key carbohydrate-recognition domains in MBPs.
  • The oligomeric state of MBPs is critical for their biological activity.

Purpose of the Study:

  • To elucidate the structural basis for the trimeric assembly of C-type lectin domains in human and rat mannose-binding proteins.

Main Methods:

  • X-ray crystallography was employed to determine the structures of MBP fragments.
  • Analysis of the crystal structures focused on the coiled-coil region and its interaction with lectin domains.

Main Results:

  • The triple-stranded alpha-helical coiled coil region was identified as the primary structural element responsible for trimerization.

Related Experiment Videos

  • This coiled coil mediates the specific trimeric orientation of the C-type lectin domains.

    • Conclusions:

    • The alpha-helical coiled coil is essential for the formation and stability of the MBP trimer.
    • Understanding this structural feature provides insights into MBP function and potential therapeutic targeting.