Billeter M, Qian Y, Otting G, Müller M, Gehring W J, Wüthrich K
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
J Mol Biol. 1990 Jul 5;214(1):183-97. doi: 10.1016/0022-2836(90)90155-f.
The determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution is described. The techniques used are 1H nuclear magnetic resonance spectroscopy for the data collection, and calculation of the protein structure with the program DISMAN followed by restrained energy minimization with a modified version of the program AMBER. A group of 19 conformers characterizes a well-defined structure for residues 7 to 59, with an average root-mean-square distance from the backbone atoms of 0.6 A relative to the mean of the 19 structures. The structure contains a helix from residues 10 to 21, a helix-turn-helix motif from residues 28 to 52, which is similar to those reported for several prokaryotic repressor proteins, and a somewhat flexible fourth helix from residues 53 to 59, which essentially forms an extension of the presumed recognition helix, residues 42 to 52. The helices enclose a structurally well-defined molecular core of hydrophobic amino acid side-chains.
本文描述了果蝇触角足同源异型域在溶液中的三维结构测定。所使用的技术包括用于数据收集的1H核磁共振光谱，以及使用DISMAN程序计算蛋白质结构，随后使用AMBER程序的修改版本进行受限能量最小化。一组19个构象异构体表征了7至59位残基的明确结构，相对于19种结构的平均值，其主链原子的平均均方根距离为0.6埃。该结构包含一个10至21位残基的螺旋，一个28至52位残基的螺旋-转角-螺旋基序，这与报道的几种原核阻遏蛋白的基序相似，以及一个53至59位残基的有点灵活的第四螺旋，它基本上形成了假定的识别螺旋（42至52位残基）的延伸。这些螺旋包围了一个结构明确的由疏水氨基酸侧链组成的分子核心。
