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A model of the structure of human annexin VI bound to lipid monolayers
Author(s) -
Driessen H.P.C.,
Newman R.H.,
Freemont P.S.,
Crumpton M.J.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80841-4
Subject(s) - annexin , annexin a2 , phospholipid , monolayer , chemistry , biophysics , calcium , biochemistry , crystallography , biology , organic chemistry , membrane , cell
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.