A model of the structure of human annexin VI bound to lipid monolayers

FEBS Letters

Freemont, P.S.²  Crumpton, M.J.³  Driessen, H.P.C.¹  Newman, R.H.³ 

[1] ICRF Unit of Structural Molecular Biology, Birkbeck College, Malet St., London, WC1E 7HX, UK;Protein Structure Laboratory, Imperial Cancer Research Fund, PO Box 123, Lincoln's Inn Fields, London, WC2A 3PX, UK;Cell Surface Biochemistry Laboratory, Imperial Cancer Research Fund, PO Box 123, Lincoln's Inn Fields, London, WC2A 3PX, UK

关键词: Annexin;    Protein structure;    Membrane;    Electron microscopy;    Phospholipid monolayer;   

DOI  :  10.1016/0014-5793(92)80841-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown