THE EFFECT OF METAL-BINDING ON THE STRUCTURE OF ANNEXIN-V AND IMPLICATIONS FOR MEMBRANE-BINDING

被引:60
作者
LEWITBENTLEY, A
MORERA, S
HUBER, R
BODO, G
机构
[1] BENDER & CO,VIENNA,AUSTRIA
[2] MAX PLANCK INST BIOCHEM,W-8033 MARTINSRIED,GERMANY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 210卷 / 01期
关键词
D O I
10.1111/j.1432-1033.1992.tb17392.x
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 structure of annexin V, crystallised in the presence of two calcium or barium ions for each protein molecule, was solved by molecular replacement to 0.24 nm resolution. The two metal ions are found in domains I and IV, i.e. on the same side of the channel that lies in the centre of the molecule. The structures of the barium and calcium form are extremely close, the only differences localised in the metal-binding sites that lie on the surface of the molecule. The occupancies of the metal ions, however, are lower for barium than for calcium, expressing the lower affinity of the protein for the former. The packing of the annexin molecules in the crystal asymmetric unit may represent a model for the calcium driven association of membrane-bound annexins that leads to membrane fusion.
引用
收藏
页码:73 / 77
页数:5
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