...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 angstrom resolution
【24h】

Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 angstrom resolution

机译：双功能玉米哈格曼因子抑制剂的结构决定因素：分辨率为1.95埃的X射线晶体结构

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

Corn Hageman factor inhibitor (CHFI) is a bifunctional 127 residue, 13.6 kDa protein isolated from corn seeds. It inhibits mammalian trypsin and Factor XIIa (Hageman Factor) of the contact pathway of coagulation as well as alpha-amylases from several insect species. Among the plasma proteinases, CHFI specifically inhibits Factor XIIa without affecting the activity of other coagulation proteinases. We have isolated CHFI from corn and determined the crystallographic structure at 1.95 Angstrom resolution. Additionally, we have solved the structure of the recombinant protein produced in Escherichia coli at 2.2 Angstrom resolution. The two proteins are essentially identical. The proteinase binding loop is in the canonical conformation for proteinase inhibitors. In an effort to understand alpha-amylase inhibition by members of the family of 25 cereal trypsin/alpha-amylase inhibitors, we have made three-dimensional models of several proteins in the family based on the CHFI coordinates and the coordinates determined for wheat alpha-amylase inhibitor 0.19 [Oda, Y., Matsunaga, T., Fukuyama, K., Miyazaki, T., and Morimoto, T. (1997) Biochemistry 36, 13503-13511]. From an analysis of the models and a structure-based sequence analysis, we propose a testable hypothesis for the regions of these proteins which bind alpha-amylase. In the course of the investigations, we have found that the cereal trypsin/alpha-amylase inhibitor family is evolutionarily related to the family of nonspecific lipid-transfer proteins of plants. This is a new addition to the group which now consists of the trypsin/alpha-amylase inhibitors, 2S seed storage albumins, and the lipid-transfer family. Apparently, the four-helix conformation has been a successful vehicle in plant evolution for providing protection from predators, food for the embryo, and lipid transfer. [References: 57]
机译：玉米哈格曼因子抑制剂（CHFI）是从玉米种子中分离出来的双功能127残基，13.6 kDa蛋白。它抑制哺乳动物的胰蛋白酶和凝血接触途径的XIIa因子（Hageman因子）以及几种昆虫的α-淀粉酶。在血浆蛋白酶中，CHFI特异性抑制XIIa因子，而不会影响其他凝血蛋白酶的活性。我们从玉米中分离出CHFI，并确定了1.95埃分辨率的晶体结构。另外，我们已经解决了在大肠杆菌中以2.2埃分辨率产生的重组蛋白的结构。两种蛋白质基本相同。蛋白酶结合环在蛋白酶抑制剂的标准构象中。为了了解25种谷物胰蛋白酶/α-淀粉酶抑制剂家族成员对α-淀粉酶的抑制作用，我们基于CHFI坐标和为小麦α-淀粉蛋白确定的坐标，建立了该家族中几种蛋白质的三维模型。淀粉酶抑制剂0.19 [Oda，Y.，Matsunaga，T.，Fukuyama，K.，Miyazaki，T。和Morimoto，T。（1997）Biochemistry 36，13503-13511]。通过对模型的分析和基于结构的序列分析，我们为结合α-淀粉酶的这些蛋白质的区域提出了可检验的假设。在调查过程中，我们发现谷物胰蛋白酶/α-淀粉酶抑制剂家族与植物的非特异性脂质转移蛋白家族进化相关。这是该组的新成员，该组现在由胰蛋白酶/α-淀粉酶抑制剂，2S种子储存白蛋白和脂质转移家族组成。显然，四螺旋构象已成为植物进化中的成功载体，可提供对天敌，胚胎食物和脂质转移的保护。 [参考：57]

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
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