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Related Experiment Videos

Ca2+-dependent structural changes in C-type mannose-binding proteins

K K Ng1, S Park-Snyder, W I Weis

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

Biochemistry
|January 28, 1999
PubMed
Summary

Calcium ions are crucial for C-type lectin function, influencing protein structure and carbohydrate binding. Their removal causes significant conformational changes, particularly in loop regions, affecting protein interactions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • C-type animal lectins are proteins mediating cell-surface carbohydrate recognition via a conserved carbohydrate-recognition domain (CRD).
  • Carbohydrate binding in most C-type lectins requires Ca2+ binding at two specific sites within the CRD.

Purpose of the Study:

  • To investigate the structural transitions in C-type lectins associated with Ca2+ binding.
  • To elucidate the role of Ca2+ in the conformational dynamics of the carbohydrate-recognition domain.

Main Methods:

  • Determined high-resolution crystal structures of rat serum mannose-binding protein (MBP) with Ho3+ (as a Ca2+ substitute).
  • Determined the crystal structure of the apo form (Ca2+-free) of rat liver MBP.
  • Compared structures to analyze conformational changes upon Ca2+ removal.

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Main Results:

  • Ca2+ removal does not alter the core CRD structure but induces significant conformational changes in loop regions.
  • A key structural change involves the isomerization of a cis-peptide bond preceding a conserved proline in Ca2+ site 2.
  • This peptide bond adopts cis in Ca2+-bound forms and both cis/trans conformations in the apo form, influencing loop conformations.

Conclusions:

  • Ca2+ binding plays a critical role in stabilizing specific loop conformations within the CRD of C-type lectins.
  • The observed structural transitions in MBPs are likely general features of Ca2+ binding across the C-type lectin family.
  • Understanding these Ca2+ dependent structural dynamics is key to deciphering lectin-carbohydrate interactions.