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Three-dimensional structure of annexins

S Liemann1, R Huber

  • 1Abteilung für Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany. liemann@mol.biol.ethz.ch

Cellular and Molecular Life Sciences : CMLS
|June 1, 1997
PubMed
Summary

Annexins are calcium-binding proteins with a conserved four-domain structure. Their interaction with phospholipid membranes, particularly their peripheral binding mode, is well-documented through various techniques.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Annexins are a family of calcium- and phospholipid-binding proteins.
  • Their molecular structure is well-characterized in crystalline and membrane-bound states.

Purpose of the Study:

  • To detail the molecular structure of annexins.
  • To investigate their binding to phospholipid membranes.

Main Methods:

  • Crystallography
  • Electron microscopy
  • Various biophysical techniques

Main Results:

  • Annexin polypeptide chains fold into four or eight similar alpha-helical domains.
  • A central hydrophilic pore is present within the annexin structure.
  • The four-domain arrangement is conserved when annexins bind to phospholipid membranes.
  • A peripheral binding mode to membranes is well-documented.

Conclusions:

  • Annexins exhibit a conserved structural organization.
  • Their interaction with membranes involves a peripheral binding mode.
  • Structural insights are crucial for understanding annexin function.

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