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Crystal structure of the annexin XII hexamer and implications for bilayer insertion

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Abstract

ANNEXINS are a family of calcium- and phospholipid-binding proteins1,2 implicated in a number of biological processes including membrane fusion3 and ion channel formation4–7. The crystal structure of the annexin XII hexamer, refined at 2.8 Å resolution, forms a concave disk with 3–2 symmetry, about 100 Å in diameter and 70 Å thick with a central hydrophilic pore. Six intermolecular Ca2+ ions are involved in hexamer formation. An additional 18 Ca2+ ions are located on the perimeter of the disk, accessible only from the side of the hexameric disk. On the basis of the hexamer structure we propose here a new mode of protein–phospholipid bilayer interaction that is distinct from the hydrophobic insertion of typical membrane proteins. This speculative model postulates the Ca2+ -dependent insertion of the hydrophilic annexin XII hexamer into phospholipid bilayers with local reorientation of the bilayer phospholipids.

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Author notes

  1. William S. Mailliard, David D. Schlaepfer and Harry T. Haigler: Department of Physiology and Biophysics, University of California, Irvine, California 92717, USA

Authors and Affiliations

  1. Stanford Synchrotron Radiation Laboratory, MS 69, Stanford, California, 94305, USA

    Hartmut Luecke, Bryna T. Chang, William S. Mailliard, David D. Schlaepfer & Harry T. Haigler

Authors
  1. Hartmut Luecke
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  2. Bryna T. Chang
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  3. William S. Mailliard
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  4. David D. Schlaepfer
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  5. Harry T. Haigler
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Luecke, H., Chang, B., Mailliard, W. et al. Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature 378, 512–515 (1995). https://doi.org/10.1038/378512a0

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  • DOI: https://doi.org/10.1038/378512a0

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