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The structure of recombinant human annexin VI in crystals and membrane-bound.
- Source :
-
Journal of molecular biology [J Mol Biol] 1996 Aug 02; Vol. 260 (5), pp. 638-43. - Publication Year :
- 1996
-
Abstract
- The crystal structure of calcium-free recombinant human annexin VI was solved at a resolution of 3.2 A by using the annexin I model for Patterson search and refined to an R-factor of 19.0%. The molecule consists of two similar halves closely resembling annexin I connected by an alpha-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.
- Subjects :
- Annexin A6 metabolism
Annexin A6 ultrastructure
Binding Sites
Calcium metabolism
Cell Membrane metabolism
Crystallization
Crystallography, X-Ray
Humans
Ion Channels metabolism
Microscopy, Electron
Models, Molecular
Patch-Clamp Techniques
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins chemistry
Annexin A6 chemistry
Protein Conformation
Subjects
Details
- Language :
- English
- ISSN :
- 0022-2836
- Volume :
- 260
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 8709144
- Full Text :
- https://doi.org/10.1006/jmbi.1996.0426