Letter | Published:

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

Nature volume 378, pages 512515 (30 November 1995) | Download Citation

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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 information

Author notes

    • William S. Mailliard
    • , David D. Schlaepfer
    •  & Harry T. Haigler

    Department of Physiology and Biophysics, University of California, Irvine, California 92717, USA

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

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

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