首页 正文

Journal of structural biology. 2016 Jul;195(1):129-38. doi: 10.1016/j.jsb.2016.02.020 Q22.72025

Structure of Leishmania donovani coronin coiled coil domain reveals an antiparallel 4 helix bundle with inherent asymmetry

利什曼原虫冠状蛋白卷曲螺旋结构域的结构揭示了反向四螺旋束的内在不对称性 翻译改进

Ashok Ranjan Nayak  1, Sharanbasappa Shrimant Karade  1, Vijay Kumar Srivastava  1, Ajay Kumar Rana  1, C M Gupta  1, Amogh A Sahasrabuddhe  1, J Venkatesh Pratap  2

作者单位 +展开

作者单位

  • 1 Division of Molecular and Structural Biology, CSIR - Central Drug Research Institute, Jankipuram Extension, Sitapur Road, Lucknow 226031, India.
  • 2 Division of Molecular and Structural Biology, CSIR - Central Drug Research Institute, Jankipuram Extension, Sitapur Road, Lucknow 226031, India. Electronic address: jvpratap@cdri.res.in.
  • DOI: 10.1016/j.jsb.2016.02.020 PMID: 26940672

    摘要 Ai翻译

    Coiled coils are ubiquitous structural motifs that serve as a platform for protein-protein interactions and play a central role in myriad physiological processes. Though the formation of a coiled coil requires only the presence of suitably spaced hydrophobic residues, sequence specificities have also been associated with specific oligomeric states. RhXXhE is one such sequence motif, associated with parallel trimers, found in coronins and other proteins. Co... ...点击完成人机验证后继续浏览
    Copyright © Journal of structural biology. 中文内容为AI机器翻译,仅供参考!

    相关内容

    期刊名:Journal of structural biology

    缩写:J STRUCT BIOL

    ISSN:1047-8477

    e-ISSN:1095-8657

    IF/分区:2.7/Q2

    文章目录 更多期刊信息

    全文链接
    引文链接
    复制
    已复制!
    推荐内容
    Structure of Leishmania donovani coronin coiled coil domain reveals an antiparallel 4 helix bundle with inherent asymmetry