Crystal structure of bovine annexin VI in a calcium-bound state.
The crystal structure of a calcium-bound form of bovine annexin VI has been determined with X-ray diffraction data to 2.9 A by molecular replacement. Six Ca2+ ions were found, five in AB loops, one in a DE loop. Two loops (II-AB, which binds calcium, and V-AB, which does not) have conformations that differ significantly from those in calcium-free, human recombinant annexin VI. There are only small differences between the calci- and the apo-annexin VI in the rest of the molecule. Calcium by itself does not promote a major conformational change.
Avila-Sakar
A J
AJ
Department of Pharmacology, University of Virginia, Charlottesville, VA 22908, USA. aa4n@virginia.edu
Creutz
C E
CE
Kretsinger
R H
RH
D017398:Alternative Splicing / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D017317:Annexin A6 / Q000737:chemistry*; D001059:Apoproteins / Q000737:chemistry; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry*; D002135:Calcium-Binding Proteins / Q000737:chemistry; D002417:Cattle; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D014961:X-Ray Diffraction
D017317:Annexin A6; D001059:Apoproteins; D002135:Calcium-Binding Proteins; D002118:Calcium