The structure of recombinant human annexin VI in crystals and membrane-bound

被引:86
作者
Benz, J [1 ]
Bergner, A [1 ]
Hofmann, A [1 ]
Demange, P [1 ]
Gottig, P [1 ]
Liemann, S [1 ]
Huber, R [1 ]
Voges, D [1 ]
机构
[1] MAX PLANCK INST BIOCHEM,ABT STRUKTURFORSCH,D-82152 MARTINSRIED,GERMANY
关键词
annexin; crystal structure; electron microscopy; ion channel activity;
D O I
10.1006/jmbi.1996.0426
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 calcium-free recombinant human annexin VI was solved at a resolution of 3.2 Angstrom by using the annexin I model for Patterson search and refined to an X-factor of 19.0%. The molecule consists of two similar halves closely resembling annexin I connected by an a-helical segment and arranged perpendicular to each other. The calcium and membrane binding sites assigned by structural homology are therefore not located in the same plane. Analysis of the membrane-bound form of annexin VI by electron microscopy shows the two halves of the molecule coplanar with the membrane, but oriented differently to the crystal structure and suggesting a flexible arrangement. Ion channel activity has been found for annexin VI and the half molecules by electrophysiological experiments. (C) 1996 Academic Press Limited
引用
收藏
页码:638 / 643
页数:6
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