期刊论文

The Structure Analysis of VLDL Receptor's Ligand-binding Domain

中文

生物信息学

1672-5565

2003

1

1

20-24

10.3969/j.issn.1672-5565.2003.01.005

国家自然科学基金（39670162）；

本校为第一机构

极低密度脂蛋白受体(VLDL-R)的配体结合域具有8个富含半胱氨酸的配体结合重复序列(ligand-binding repeats,LBR),被认为是与配体结合的部位.该受体与含7个类似重复序列的低密度脂蛋白受体(LDL-R)的配体结合特性明显不同.为了明确VLDL-R中8个LBR在配体结合中的作用并探讨结合位点的结构,本研究采用计算机辅助蛋白质结构预测方法,在二级结构分析的基础上,通过同源建模方法预测受体N-端328个氨基酸的配体结合域空间结构,结果显示该区域呈现弧形口袋样结构,其中前3个LBR结构紧凑,呈棒状,负电荷相对集中,推测这一特征结构是配体结合的重要结构基础,结构分析同时表明在LBR5与LBR6之间连接区的弹性结构...

The ligand - binding domain of the very low - density lipoprotein receptor( VLDL - R) contains eight cysteine - rich repeal sequences that have been postulated as place for ligand - binding. Its binding characterise is obviously different from that of low - density lipoprotein receptor( LDL - R) with seven similar repeats. To make clear the contribution of these repeats to ligand- binding and to explore the ligand- binding rites' structure, the method of protein structure prediction were adapted to analysize the 328 amino acids sequence of the receptor' N - end which showed an arc pocket - lik...