• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文会议>International Conference on Fundamental and Applied Sciences >Peptide docking of HIV-1 p24 with single chain fragment variable (scFv) by CDOCKER Algorithm
【24h】

Peptide docking of HIV-1 p24 with single chain fragment variable (scFv) by CDOCKER Algorithm

机译：通过CDOCKER算法将HIV-1 P24与单链片段变量（SCFV）进行肽对接

获取原文
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

In search for the important residues that might have involve in the binding interaction between the p24 caspid protein of HIV-1 fragment (MET68 - PRO90) with the single chain fragment variable (scFv) of FAB23.5, modern computational chemistry approach has been conducted and applied. The p24 fragment was initially taken out from the 1AFV protein molecule consisting of both light (V_L) and heavy (V_H) chains of FAB23.5 as well as the HIV-1 caspid protein. From there, the p24 (antigen) fragment was made to dock back into the protein pocket receptor (antibody) by using the CDOCKER algorithm to conduct the molecular docking process. The score calculated from the CDOCKER gave 15 possible docked poses with various docked ligand's positions, the interaction energy as well as the binding energy. The best docked pose that imitates the original antigen's position was determined and further processed to the In Situ minimization to obtain the residues interaction energy as well as to observe the hydrogen bonds interaction in the protein-peptide complex. Based on the results demonstrated, the specific residues in the complex that have shown immense lower interaction energies in the 5? vicinity region from the peptide are from the heavy chain (VH:TYR105) and light chain (VL:ASN31, TYR32, and GLU97). Those residues play vital roles in the binding mechanism of Antibody- Antigen (Ab-Ag) complex of p24 with FAB23.5.
机译：在寻找可能涉及HIV-1片段（MET68-PRO90）的P24胱天脂蛋白（MET68-PRO90）与FAB23.5的单链片段变量（SCFV）之间的结合相互作用的重要残留物，已经进行了现代计算化学方法并应用。最初从一个由Fab23.5的光（V_L）和重（V_H）链和HIV-1胱氨酸蛋白组成的1AFV蛋白质分子中取出P24片段。从那里，通过使用CDOCKER算法进行分子对接过程，使P24（抗原）片段靠回蛋白质口袋受体（抗体）。从CDOCKER计算的分数给出了15个可能的对接的姿势，具有各种停靠配体的位置，相互作用能量以及绑定能量。确定仿原始抗原位置的最佳停靠姿势并进一步加工到原位最小化，以获得残留物相互作用能量，以及观察蛋白肽复合物中的氢键相互作用。基于结果证明，复合物中的特定残留物在5中显示了巨大的较低的相互作用能量？来自肽的附近区域来自重链（VH：Tyr105）和轻链（VL：Asn31，Tyr32和Glu97）。这些残留物在P24的P23的抗体抗原（AB-AG）复合物的结合机制中起重要作用。

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