Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis.
Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis.
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DOI：
10.1016/s0006-3495(95)79894-0
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发表时间：
1995-07
影响因子：
3.4
通讯作者：
Markus Tempel;H. Wolfgang;Goldmann;Gerhard Isenberg;Erich Sackmann
中科院分区：
文献类型：
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作者：
Markus Tempel;H. Wolfgang;Goldmann;Gerhard Isenberg;Erich Sackmann
在最近的体外实验中，已经证明Talin分子的47 kDa片段和vinculin分子的32 kDa片段与酸性磷脂相互作用。通过计算机分析的方法，我们确定了这些片段的疏水和两亲性伸展，并应用专门编写的矩阵方法，确定了α-螺旋的分子两亲性结构。对47 kDa的小鼠Talin片段(残基1-433；NH2-末端区域)的计算表明，残基21-39、287-342和385-406与酸性磷脂以及小鼠Talin(初级氨基酸序列385-401)和Dictyostelialin(初级氨基酸序列348-364)的一般脂结合区域具有特异性相互作用。对32 kDa鸡胚纽蛋白片段(残基858-1066；COOH-末端区域)和线虫纽蛋白序列的计算表明，鸡胚纽蛋白残基935-978和1020-1040与酸性磷脂相互作用。纽菌素(残留物916-970)的实验已经得到证实，现在需要进一步的详细实验分析来支持剩余的计算数据。
In recent in vitro experiments, it has been demonstrated that the 47-kDa fragment of the talin molecule and the 32-kDa fragment of the vinculin molecule interact with acidic phospholipids. By using a computer analysis method, we determined the hydrophobic and amphipathic stretches of these fragments and, by applying a purpose-written matrix method, we ascertained the molecular amphipathic structure of alpha-helices. Calculations for the 47-kDa mouse talin fragment (residues 1–433; NH2-terminal region) suggest specific interactions of residues 21–39, 287–342, and 385–406 with acidic phospholipids and a general lipid-binding domain for mouse talin (primary amino acid sequence 385–401) and for Dictyostelium talin (primary amino acid sequence 348–364). Calculations for the 32-kDa chicken embryo vinculin fragment (residues 858–1066; COOH-terminal region) and from nematode vinculin alignment indicate for chicken embryo vinculin residues 935–978 and 1020–1040 interactions with acidic phospholipids. Experimental confirmation has been given for vinculin (residues 916–970), and future detailed experimental analyses are now needed to support the remaining computational data.