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Related Experiment Videos

Variable zinc coordination in endostatin.

E Hohenester1, T Sasaki, K Mann

  • 1Biophysics Section, Blackett Laboratory, Imperial College, London, SW7 2AZ, UK. hohenester@ic.ac.uk

Journal of Molecular Biology
|March 8, 2000
PubMed
Summary
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Zinc binding in mouse endostatin, an angiogenesis inhibitor, shows structural flexibility. This suggests zinc plays a structural role, not a critical functional one, in endostatin

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cancer Research

Background:

  • Endostatin, a collagen XVIII fragment, inhibits angiogenesis and tumor growth.
  • The role of a bound zinc ion in endostatin's anti-tumor activity is debated.
  • Previous studies noted zinc in human endostatin but not mouse endostatin at pH 5.

Purpose of the Study:

  • To investigate the structural characteristics and zinc-binding properties of mouse endostatin.
  • To clarify the role of zinc in endostatin's structure and function.

Main Methods:

  • Determined two new crystal structures of mouse endostatin at pH 8.5 with bound zinc.
  • Utilized site-directed mutagenesis of zinc-binding residues.
  • Analyzed zinc coordination geometries in solution.

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Main Results:

  • Identified two distinct zinc coordination geometries in mouse endostatin crystal structures.
  • One structure mimicked human endostatin's zinc binding, while the other showed altered ligand involvement (Asp136 replacing His132).
  • Mutagenesis confirmed that both coordination modes are possible in solution.

Conclusions:

  • Mouse endostatin exhibits significant structural heterogeneity in its zinc-binding site.
  • The observed flexibility in zinc coordination suggests a primarily structural role for zinc.
  • Zinc is unlikely to be critical for endostatin's anti-tumor function.