Kobayashi Y, Ohkubo T, Kyogoku Y, Koyama S, Kobayashi M, Go N
Institute for Protein Research, Osaka University.
J Biochem. 1988 Sep;104(3):322-5. doi: 10.1093/oxfordjournals.jbchem.a122466.
The three-dimensional structure of alpha-human ANP in solution was determined through the combined use of nuclear magnetic resonance spectroscopy and distance geometry. The results are based on distance constraints determined by nuclear Overhauser effect measurements and one disulfide bond. The structure is as follows. Three separate regions, which are Ser1-Cys7, Arg11-Ile15, and Gln18-Tyr28 each have some ordered structure. The remaining parts in the sequences of Gly9-Gly10 and Gly16-Ala17 act as hinges. And the C-terminal part is folded back toward the cyclic moiety. The conformation of alpha-hANP reported here is expected to give a better understanding of the relationships between its biological activities and three-dimensional structure.
通过结合使用核磁共振光谱法和距离几何方法，确定了溶液中α-人心钠素的三维结构。结果基于通过核Overhauser效应测量确定的距离限制和一个二硫键。结构如下。三个独立的区域，即Ser1-Cys7、Arg11-Ile15和Gln18-Tyr28各自具有一些有序结构。序列中Gly9-Gly10和Gly16-Ala17的其余部分起铰链作用。并且C末端部分向环状部分折叠回来。本文报道的α-hANP的构象有望更好地理解其生物活性与三维结构之间的关系。
