The crystal structure of annexin VI indicates relative rotation of the two lobes upon membrane binding.
The crystal structure of annexin VI indicates relative rotation of the two lobes upon membrane binding.
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膜联蛋白 VI 的晶体结构表明膜结合时两个叶的相对旋转。
DOI：
10.1016/0167-4889(96)00100-0
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Kretsinger,RH
中科院分区：
文献类型：
--
作者：
Kawasaki,H;Avila-Sakar,A;Creutz,CE;Kretsinger,RH
用分子置换法对牛肝膜联蛋白VI的晶体结构进行了低分辨测定。第一叶(域1-4)相对于第二叶(域5-8)旋转约90°。由于相同的晶型(P43，68×68×205Å)由(NH_4)_2SO_4、聚乙二醇和乙酸钠在加和不加钙的情况下生长，这可能反映了溶液中的结构。当与脂单分子层结合时，膜联蛋白VI的两个叶是共面的。这意味着结合到膜上时构象发生了显著的变化。
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° relative to the second lobe (domains 5–8). Since the same crystal form (P 43, 68 × 68 × 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.