Crystal structure of bovine annexin VI in a calcium-bound state

被引:49
作者
Avila-Sakar, AJ [1 ]
Creutz, CE
Kretsinger, RH
机构
[1] Univ Virginia, Dept Pharmacol, Charlottesville, VA 22908 USA
[2] Univ Virginia, Dept Biol, Charlottesville, VA 22908 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1387卷 / 1-2期
关键词
annexin; calcium; X-ray crystallography;
D O I
10.1016/S0167-4838(98)00111-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of a calcium-bound form of bovine annexin VI has been determined with X-ray diffraction data to 2.9 Angstrom 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. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:103 / 116
页数:14
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