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Trimeric structure of a C-type mannose-binding protein

W I Weis1, K Drickamer

  • 1Department of Structural Biology, Stanford University School of Medicine, CA 94305.

Structure (London, England : 1993)
|December 15, 1994
PubMed
Summary
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Mannose-binding proteins (MBPs) are serum lectins that bind pathogens. Structural studies reveal their carbohydrate-binding sites are spaced too far apart for single trimers to bind typical mammalian sugars, enabling selective pathogen recognition.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Mannose-binding proteins (MBPs) are Ca(2+)-dependent animal lectins found in serum.
  • MBPs recognize oligosaccharide structures on pathogenic bacteria and fungi to neutralize them.
  • MBPs exhibit weak affinity for monovalent sugars but strong binding to multivalent ligands.

Purpose of the Study:

  • To elucidate the structure and binding characteristics of mannose-binding protein A (MBP-A).
  • To understand the molecular basis for selective pathogen recognition by MBPs.

Main Methods:

  • Solution-based physical studies.
  • X-ray crystallography to determine the structure of an MBP-A fragment at 1.8 Å resolution.
  • Sequence alignments of related C-type lectins.

Related Experiment Videos

Main Results:

  • The crystal structure of an MBP-A fragment revealed a trimeric carbohydrate-recognition domain (CRD) linked to a neck domain forming a triple-stranded coiled coil.
  • The neck domain alone did not form stable helices in aqueous solution.
  • Carbohydrate-binding sites on the trimer are separated by 53 Å.

Conclusions:

  • The wide spacing of binding sites in MBP-A prevents binding to typical mammalian oligosaccharides but allows avid binding to repetitive sugar arrays on pathogens.
  • This spacing mechanism enables selective pathogen recognition by MBPs.
  • Other C-type lectins likely share similar oligomeric structures, with variations influencing their specific oligosaccharide interactions.