A model of the structure of human annexin VI bound to lipid monolayers
- 13 July 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 306 (1) , 75-79
- https://doi.org/10.1016/0014-5793(92)80841-4
Abstract
Annexin VI is an eight repeat member of the annexin family of proteins which are both water soluble and bind to negatively charged phospholipids in a calcium-dependent manner. Here we present a model for annexin VI based on fitting the three-dimensional structure of two annexin V molecules (Huber (1990) EMBO J. 9, 3867–23;874) to the two-dimensional stain-excluding density of lipid-bound annexin VI (Newman (1989) J. Mol. Biol. 206, 213–219). Both annexin VI lobes could only be fitted with their convex faces closest to the lipid monolayer. This supports the hypothesis that annexin—lipid binding is mediated by the interaction between calcium bound to the loops protruding from the convex protein surface and phospholipid headgroups.Keywords
This publication has 23 references indexed in Scilit:
- Crystal and molecular structure of human annexin V after refinement: Implications for structure, membrane binding and ion channel formation of the annexin family of proteinsJournal of Molecular Biology, 1992
- Microcrystals of the annexin, p68: Paracrystal to crystal transition and molecular packing as determined by electron microscopy and image reconstructionJournal of Structural Biology, 1991
- Structure of soluble and membrane-bound human annexin VJournal of Molecular Biology, 1991
- Amino acid sequence analysis of the annexin super‐gene family of proteinsEuropean Journal of Biochemistry, 1991
- 2D crystal forms of annexin IV on lipid monolayersFEBS Letters, 1991
- Sub-domain structure of lipid-bound annexin-V resolved by electron image analysisJournal of Molecular Biology, 1991
- The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution Implications for membrane binding and calcium channel activityFEBS Letters, 1990
- Synexin (annexin VII): A cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranesThe Journal of Membrane Biology, 1990
- Crystallization of p68 on lipid monolayers and as three-dimensional single crystalsJournal of Molecular Biology, 1989
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983