[PDF][PDF] The structure of recombinant human annexin VI in crystals and membrane-bound

J Benz, A Bergner, A Hofmann, P Demange… - Journal of molecular …, 1996 - academia.edu
J Benz, A Bergner, A Hofmann, P Demange, P Göttig, S Liemann, R Huber, D Voges
Journal of molecular biology, 1996academia.edu
Strukturforschung, D-82152 search and refined to an R-factor of 19.0%. The molecule
consists of two Martinsried, Germany similar halves closely resembling annexin I connected
by an a-helical segment and arranged perpendicular to each other. The calcium and
membrane binding sites assigned by structural homology are therefore not located in the
same plane. Analysis of the membrane-bound form of annexin VI by electron microscopy
shows the two halves of the molecule coplanar with the membrane, but oriented differently to …
Strukturforschung, D-82152 search and refined to an R-factor of 19.0%. The molecule consists of two Martinsried, Germany similar halves closely resembling annexin I connected by an a-helical segment and arranged perpendicular to each other. The calcium and membrane binding sites assigned by structural homology are therefore not located in the same plane. Analysis of the membrane-bound form of annexin VI by electron microscopy shows the two halves of the molecule coplanar with the membrane, but oriented differently to the crystal structure and suggesting a flexible arrangement. Ion channel activity has been found for annexin VI and the half molecules by electrophysiological experiments.
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