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The crystal structure of annexin VI indicates relative rotation of the two lobes upon membrane binding.

Authors :
Kawasaki H
Avila-Sakar A
Creutz CE
Kretsinger RH
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