1aei
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(New page: 200px<br /><applet load="1aei" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aei, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 08:40, 20 November 2007
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CRYSTAL STRUCTURE OF THE ANNEXIN XII HEXAMER
Overview
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.
About this Structure
1AEI is a Single protein structure of sequence from Hydra vulgaris with CA as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the annexin XII hexamer and implications for bilayer insertion., Luecke H, Chang BT, Mailliard WS, Schlaepfer DD, Haigler HT, Nature. 1995 Nov 30;378(6556):512-5. PMID:7477411
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