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

Author

Luecke, Hartmurt, Chang, Bryna T., Mailliard, William S., Schlaepfer, David D., and Haigler, Harry T.

Subjects
Proteins -- Structure, Bilayer lipid membranes -- Research, Calcium ions -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

The 2.8 angstrom resolution atomic structure of the annexin XII hexamer reveals a 210K homohexamer with 3-2 symmetry in the asymmetric unit. The 70-angstrom-thick hexamer forms a concave disk with a diameter of 100 angstroms. Six Ca2+ ions are present in the hexamer formation. A novel model for annexin-phospholipid bilayer interaction indicates that Ca2+ sites present on the perimeter of the hexamer regulate the hydrophilic insertion of the protein complex into the phospholipid layer.

Published
1995

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