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Related Experiment Videos

Annexin V-crystal structure and its implications on function.

R Huber1, R Berendes, A Burger

  • 1Max-Planck-Institut für Biochemie, Martinsried, Germany.

Behring Institute Mitteilungen
|April 1, 1992
PubMed
Summary
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Annexin V, a Janus-faced protein, forms calcium-dependent ion channels. Its structure reveals a central pore and phospholipid binding sites, explaining its membrane interaction and ion transport capabilities.

Area of Science:

  • Structural biology
  • Biophysics
  • Membrane protein research

Background:

  • Annexins are soluble proteins binding phospholipids in a calcium-dependent manner.
  • They exhibit properties of both soluble and integral membrane proteins.
  • Annexins mediate ion transport and interact with cell membranes.

Purpose of the Study:

  • To present the refined structure and molecular model of annexin V.
  • To elucidate the mechanism of annexin V's membrane interaction and ion channel formation.
  • To describe the electrophysiology of annexins.

Main Methods:

  • X-ray crystallography at 2.0 A resolution.
  • Molecular modeling.
  • Electron microscopy.
  • Electrophysiological recordings.

Related Experiment Videos

Main Results:

  • Annexin V is primarily alpha-helical with four similar structural domains in a cyclic array.
  • A central hydrophilic pore, likely a calcium-selective channel, was identified.
  • Calcium binding sites on the convex face suggest phospholipid interaction and membrane anchoring.
  • Ion permeation occurs in discrete, voltage-regulated conductance states.

Conclusions:

  • The structure of annexin V explains its Janus-faced nature and membrane interaction.
  • A model for annexin V-mediated ion channel formation and conduction is proposed.
  • Annexin V functions as a calcium-dependent ion channel regulated by membrane voltage.