Annexin XII

3D print of Annexin B12 Trimer and Monomer created from protein dataset PDB ID: 1AEI; CRYSTAL STRUCTURE OF THE ANNEXIN XII HEXAMER

Protein Description

“Annexins are a family of calcium- and phospholipid-binding proteins implicated in a number of biological processes including membrane fusion and ion channel formation. The crystal structure of the annexin XII hexamer, refined at 2.8 A resolution, forms a concave disk with 3-2 symmetry, about 100 A in diameter and 70 A 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 Ca(2+)-dependent insertion of the hydrophilic annexin XII hexamer into phospholipid bilayers with local reorientation of the bilayer phospholipids.”

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3D print preview of Annexinin XII visualized as a 3D print in full-color sandstone. Colored by protein chain (Cyan, Yellow, Green) and repeat active sites AB: Red, DE: Magenta. Available in multiple sizes.

Annexin XII Hexamer

Annexin XII Monomer Volumetric Surface

Protein

Base

Annexin XII Monomer Ribbon Backbone

Protein

Base