文章摘要
韩丽萍,常平安,冉 凤,孙兰茜,王 玲,王超颖,黄飞飞.小鼠跨膜蛋白68 编码基因的克隆与分析[J].广东农业科学,2015,42(20):125-128
查看全文    HTML 小鼠跨膜蛋白68 编码基因的克隆与分析
Cloning and analysis of encoding cDNA sequenceof mouse transmembrane protein 68
  
DOI:
中文关键词: 跨膜蛋白68  小鼠  编码序列  结构
英文关键词: transmembrane protein 68  mouse  encoding sequence  structure
基金项目:重庆市基础与前沿研究项目(cstc2013 jcyjA10005,cstc2014jcyjA10033);重庆市教委科学技术 研究项目(KJ1400424);重庆市大学生创新创业训练计 划项目(201410617012)
作者单位
韩丽萍,常平安,冉 凤,孙兰茜,王 玲,王超颖,黄飞飞 重庆邮电大学生物信息学院重庆 400065 
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中文摘要:
      跨膜蛋白68(TP68)是一个结构和功能未知的蛋白。采用逆转录PCR 的方法克隆了TP68 编码 cDNA 序列,并对其进行了生物信息学分析。研究发现,小鼠TP68 编码cDNA 全长990 bp,编码329 个氨基 酸;结构域分析显示小鼠TP68 具有典型的甘油磷脂酰基转移酶结构域,并含有2 个跨膜结构域,很可能是内 质网上的一种膜蛋白;序列比对和三维建模表明其具有典型的甘油磷脂酰基转移酶的底物结合位点和催化 位点以及空间构象。这些结果首次鉴定了小鼠TP68 的编码cDNA 序列,为进一步研究其结构和功能奠定了 基础。
英文摘要:
      Transmembrane protein 68(TP68)is protein with unknown structure and function. In the present study,the coding cDNA sequence of mouse TP68 was cloned by reverse transcription PCR and analyzed by bioinformatical tools in detail. The results showed that the full length coding cDNA of mouse TP68 was 990 bp,which encoded 329 amino acids. Protein domain analysis indicated that mouse TP68 had a classical glycerophospholipid acyltransferase domain and two transmembrane domains,which may be an endoplasmic reticulum-anchored protein. Moreover,TP68 had classic substrate binding sites,catalytic active sites and spatial conformation of glycerophospholipid acyltransferases by sequence alignment and the 3-D modeling. These results for the first time identify the encoding cDNA sequence of mouse TP68 and provide the basis to further study its structure and function.
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