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Related Experiment Videos

Collectin structure: a review.

K Håkansson1, K B Reid

  • 1Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana 61801, USA. kjell@scs.uiuc.edu

Protein Science : a Publication of the Protein Society
|October 25, 2000
PubMed
Summary
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Collectins are calcium-dependent proteins that bind to pathogen carbohydrates, aiding immune clearance. Structural analysis reveals key interactions in their carbohydrate-binding domains, influencing pathogen recognition.

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Collectins are calcium-dependent lectins crucial for innate immunity.
  • They recognize carbohydrate structures on pathogens, mediating clearance.
  • Collectins possess a multimeric structure with distinct functional domains.

Purpose of the Study:

  • To elucidate the structural basis of carbohydrate recognition by collectins.
  • To understand the role of structural features in collectin function.
  • To compare structural aspects of different collectins like MBP and SP-D.

Main Methods:

  • Analysis of crystallographic data for mannan binding protein (MBP) and lung surfactant protein D (SP-D).
  • Homology modeling for collagen-like regions.

Related Experiment Videos

  • Structural characterization of collectin-carbohydrate complexes.

    • Main Results:

    • Collectin binding involves calcium ions interacting with adjacent carbohydrate hydroxyl groups.
    • Hydrogen bonding between hydroxyl groups and calcium ligands contributes to binding.
    • Structural deviations from threefold symmetry in SP-D may affect binding properties.

    Conclusions:

    • Collectin structure, particularly the lectin domain, is critical for pathogen recognition.
    • Calcium-dependent carbohydrate binding is a conserved mechanism.
    • Structural variations influence the functional specificity of collectins in host defense.