...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Spectrochimica acta, Part A. Molecular and biomolecular spectroscopy >Conformation study of HA(306-318) antigenic peptide of the haemagglutinin influenza virus protein
【24h】

Conformation study of HA(306-318) antigenic peptide of the haemagglutinin influenza virus protein

机译：血凝素流感病毒蛋白HA（306-318）抗原肽的构象研究

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

Several HLA-DR alleles present the immunodominant HA(306-318) peptide of haemagglutinin of the influenza virus to T cells. NMR data of the peptide in various water solutions exclude any a-helix or turn conformations. Circular dichroism and Fourier transform infrared spectroscopies indicate an estimated P-extended structure in water of 31% and 28%, respectively, with spectra shape similar to the ones observed for P-sheet containing proteins. The H/D amide exchange suggests a stable length-dependent interchain hydrogen-bonding. The partially P-extended conformation of HA(306-318) in solution might be close to the one found in HA(306-318)-HLA-DR1 complex. These results suggest different interconverting extended conformations of HA(306-318), depending on the microenvironment of the solution medium. This flexibility emphasizes the ability of some peptides to fit more easily the binding site of several HLA-DR molecules. Similar results were obtained on the HIV P25(263-277) peptide which has been previously shown to be a good DR binder.
机译：几个HLA-DR等位基因将流感病毒血凝素的免疫优势HA（306-318）肽呈递给T细胞。在各种水溶液中肽的NMR数据不包括任何α-螺旋或转角构象。圆二色性和傅立叶变换红外光谱表明，水中的P扩展结构估计分别为31％和28％，其光谱形状类似于包含蛋白质的P-sheet所观察到的光谱形状。 H / D酰胺交换表明稳定的长度依赖性链间氢键。 HA（306-318）在溶液中的部分P延伸构象可能与HA（306-318）-HLA-DR1复合物中发现的构象接近。这些结果表明，取决于溶液介质的微环境，HA（306-318）的相互转换扩展构象不同。这种灵活性强调了某些肽更容易适应几个HLA-DR分子结合位点的能力。在HIV P25（263-277）肽上获得了相似的结果，该肽先前已证明是良好的DR结合物。

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