膜联蛋白VI的晶体结构表明，两个叶在与膜结合时会发生相对旋转。

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

作者信息

Kawasaki H, Avila-Sakar A, Creutz C E, Kretsinger R H

机构信息

Department of Biology, University of Virginia, Charlottesville 22903, USA.

出版信息

Biochim Biophys Acta. 1996 Oct 11;1313(3):277-82. doi: 10.1016/0167-4889(96)00100-0.

DOI:10.1016/0167-4889(96)00100-0

PMID:8898865

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.

摘要

通过分子置换法已将牛肝膜联蛋白VI的晶体结构解析至低分辨率。第一叶（结构域1 - 4）相对于第二叶（结构域5 - 8）旋转了约90度。由于相同的晶体形式（P4(3)，68×68×205 Å）在添加和不添加钙的情况下均能从硫酸铵、聚乙二醇和醋酸钠中生长出来，这可能反映了其在溶液中的结构。当与脂质单层结合时，膜联蛋白VI的两个叶是共面的。这意味着在与膜结合时构象发生了显著变化。