Betton J M, Martineau P, Saurin W, Hofnung M
Département des Biotechnologies, Institut Pasteur, Paris, France.
FEBS Lett. 1993 Jun 28;325(1-2):34-8. doi: 10.1016/0014-5793(93)81409-s.
In a previous study [(1987) J. Mol. Biol. 194, 663-673], we isolated ten insertion/deletion mutants (indels) of the maltose binding protein for which the maltose binding constant was only a little or not at all affected. In this paper, we have localized these mutations in the recently solved three-dimensional structure. Contrary to the general expectation, most of the insertion/deletion modifications occurred within elements of secondary structure. An analysis of the inserted residues for three indels found within alpha helices allowed an interpretation regarding protein structure accommodation to such modifications.
在之前的一项研究中[(1987年)《分子生物学杂志》194卷,663 - 673页],我们分离出了麦芽糖结合蛋白的十个插入/缺失突变体(插入缺失),其麦芽糖结合常数仅受到轻微影响或根本未受影响。在本文中,我们已将这些突变定位到最近解析出的三维结构中。与一般预期相反,大多数插入/缺失修饰发生在二级结构元件内。对在α螺旋中发现的三个插入缺失的插入残基进行分析,有助于就蛋白质结构如何适应此类修饰做出解释。