Quax-Jeuken Y E, Quax W J, Bloemendal H
Proc Natl Acad Sci U S A. 1983 Jun;80(12):3548-52. doi: 10.1073/pnas.80.12.3548.
The nucleotide sequence of two recombinant plasmids containing hamster vimentin cDNA was determined. The sequence comprises 1,640 base pairs and reveals virtually the total primary structure of vimentin and a large part of the 3' noncoding region. Secondary structure prediction methods allow the characterization of two distinct regions of the polypeptide chain, 135 and 145 residues long, which are able to form alpha helices organized in "coiled coils." Three nonhelical domains can be distinguished: a very basic NH2-terminal domain of at least 67 residues, a nonhelical region of 45 amino acids separating the two helix domains, and a COOH-terminal region of 55 residues, which contains an excess of acidic amino acids. The meaning of each of these domains of the vimentin polypeptide for the subunit and filament formation is discussed.
测定了两个含有仓鼠波形蛋白cDNA的重组质粒的核苷酸序列。该序列由1640个碱基对组成，几乎揭示了波形蛋白的全部一级结构以及3'非编码区的大部分。二级结构预测方法能够对多肽链的两个不同区域进行表征，这两个区域分别长135和145个残基，能够形成以“卷曲螺旋”形式组织的α螺旋。可以区分出三个非螺旋结构域：一个至少有67个残基的非常碱性的NH2末端结构域、一个分隔两个螺旋结构域的45个氨基酸的非螺旋区域以及一个含有过量酸性氨基酸的55个残基的COOH末端区域。文中讨论了波形蛋白多肽的每个这些结构域对于亚基和丝状物形成的意义。
