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The crystal structure of annexin VI indicates relative rotation of the two lobes upon membrane binding.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 1996 Oct 11; Vol. 1313 (3), pp. 277-82. - Publication Year :
- 1996
-
Abstract
- The crystal structure of bovine liver annexin VI has been determined to low resolution by molecular replacement. The first lobe (domains 1-4) is rotated about 90 degrees relative to the second lobe (domains 5-8). Since the same crystal form (P4(3), 68 X 68 X 205 A) grew from (NH4)2SO4, polyethylene glycol, and sodium acetate with and without added calcium, this probably reflects the structure in solution. When bound to a lipid monolayer both lobes of annexin VI are coplanar. This implies a significant change in conformation upon binding to membranes.
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1313
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 8898865
- Full Text :
- https://doi.org/10.1016/0167-4889(96)00100-0