...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases
【24h】

An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases

机译：子域的分析定位,构象变化和紊乱有关水晶包装天门冬氨酸蛋白酶

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The analysis reported here describes detailed structural studies of endothiapepsin (the aspartic proteinase from Endothia parasitica), with and without bound inhibitors, and human pepsin 3b. Comparison of multiple crystal structures of members of the aspartic proteinase family has revealed small but significant differences in domain orientation in different crystal forms. In this paper, it is shown that these differences in domain orientation do not necessarily correlate with the presence or absence of bound inhibitors, but appear to stem at least partly from crystal contacts mediated by sulfate ions. However, since the same inherent flexibility of the structure is observed for other enzymes in this family such as human pepsin, the native structure of which is also reported here, the observed domain movements may well have implications for the mechanism of catalysis.
机译：这里的分析报告详细描述了endothiapepsin(结构研究天冬氨酸的蛋白酶从Endothia parasitica),如果没有绑定抑制剂,和人类胃蛋白酶3 b。天门冬氨酸蛋白酶的结构成员家人透露虽小但意义重大域差异在不同的方向晶体形态。这些差异在域取向不必然存在或关联缺乏一定的抑制剂,但似乎阻止至少部分由水晶接触硫酸盐离子。灵活性的结构观察这个家庭中的其他一些比如人类胃蛋白酶,本机结构也报道,观察到的域运动很有影响的机理催化。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号