title: A model of the structure of human annexin VI bound to lipid monolayers.
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, 3867-3874) 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.
authors.affiliation: ICRF Unit of Structural Molecular Biology, Birkbeck College, London, UK.
authors.forename: H P
authors.initials: HP
authors.lastname: Driessen
authors.forename: R H
authors.initials: RH
authors.lastname: Newman
authors.forename: P S
authors.initials: PS
authors.lastname: Freemont
authors.forename: M J
authors.initials: MJ
authors.lastname: Crumpton
mesh_terms: D017317:Annexin A6; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D005583:Fourier Analysis; D006801:Humans; D008958:Models, Molecular; D010743:Phospholipids / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D017317:Annexin A6; D002135:Calcium-Binding Proteins; D010743:Phospholipids