...
  • 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 >Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom.
【24h】

Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom.

机译：结构重组类型v 2 2.0埃解析:过敏的结构分析从黄蜂毒透明质酸酶。

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

Wasp venom from Vespula vulgaris contains three major allergens: Ves v 1, Ves v 2 and Ves v 5. Here, the cloning, expression, biochemical characterization and crystal structure determination of the hyaluronidase Ves v 2 from family 56 of the glycoside hydrolases are reported. The allergen was expressed in Escherichia coli as an insoluble protein and refolded and purified to obtain full enzymatic activity. Three N-glycosylation sites at Asn79, Asn99 and Asn127 were identified in Ves v 2 from a natural source by enzymatic digestions combined with MALDI-TOF mass spectrometry. The crystal structure of recombinant Ves v 2 was determined at 2.0 A resolution and reveals a central (beta/alpha)(7) core that is further stabilized by two disulfide bonds (Cys19-Cys308 and Cys185-Cys197). Based on sequence alignments and structural comparison with the honeybee allergen Api m 2, it is proposed that a conserved cavity near the active site is involved in binding of the substrate. Surface epitopes and putative glycosylation sites have been compared with those of two other major group 2 allergens from Apis mellifera (honeybee) and Dolichovespula maculata (white-faced hornet). The analysis suggests that the harboured allergic IgE-mediated cross-reactivity between Ves v 2 and the allergen from D. maculata is much higher than that between Ves v 2 and the allergen from A. mellifera.
机译：黄蜂毒从Vespula寻常的包含三个主要过敏原:大v 1,类型v类型2和5。克隆、表达、生化表征及晶体结构决心的透明质酸酶类型v 2家庭56个糖苷水解酶报道。大肠杆菌作为不溶性蛋白质和复合和纯化获得完整的酶活动。Asn99和Asn127类型v 2中被识别天然来源的酶来进行的总和MALDI-TOF质谱。结构重组类型v 2确定2.0在分辨率和显示一个中央(β/α)(7)进一步稳定的核心由两个二硫键(Cys19-Cys308和Cys185-Cys197)。与蜜蜂过敏原结构比较Api m 2,提出了守恒的腔活性部位附近参与绑定的底物。糖基化位点相比另外两个主要的组2过敏原从apimellifera(蜜蜂)和Dolichovespula maculata(面容苍白的大黄蜂)。包庇过敏的ige类型之间的大v 2和过敏原从d maculata比这高得多大v 2和蜜蜂的过敏原。

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