Finbow M E, Eliopoulos E E, Jackson P J, Keen J N, Meagher L, Thompson P, Jones P, Findlay J B
Beatson Institute for Cancer Research, Glasgow, UK.
Protein Eng. 1992 Jan;5(1):7-15. doi: 10.1093/protein/5.1.7.
A 16 kDa protein has been isolated in a homogeneous form as the major component of a paracrystalline paired membrane structure closely resembling the gap junction. The primary structure of this protein from arthropod and vertebrate species has been determined by protein and cDNA sequencing. The amino acid sequences are highly conserved and virtually identical to the amino acid sequence of the proteolipid subunit of the vacuolar H(+)-ATPases. The disposition of the protein in the membrane has been studied using proteases and the N,N'-dicyclohexylcarbodiimide reactive site identified. These data, together with secondary structure predictions, suggest that the 16 kDa protein is for the most part buried in the membrane, arranged in a bundle of four hydrophobic alpha-helices. Using computer graphics, a model has been constructed based on this arrangement and on the electron microscopic images of the paracrystalline arrays.
一种16千道尔顿的蛋白质已以均一形式分离出来，它是一种与间隙连接极为相似的副晶状成对膜结构的主要成分。已通过蛋白质和cDNA测序确定了来自节肢动物和脊椎动物物种的这种蛋白质的一级结构。氨基酸序列高度保守，实际上与液泡H(+) - ATP酶的蛋白脂质亚基的氨基酸序列相同。已使用蛋白酶研究了该蛋白质在膜中的分布，并确定了N,N'-二环己基碳二亚胺反应位点。这些数据与二级结构预测一起表明，16千道尔顿的蛋白质大部分埋在膜中，排列成一束四个疏水α-螺旋。利用计算机图形学，基于这种排列和副晶状阵列的电子显微镜图像构建了一个模型。
