STRUCTURAL BIOLOGY OF HUMAN UBIQUITIN E3 LIGASES AND INTERACTING FACTORS

人类泛素 E3 连接酶和相互作用因子的结构生物学

基本信息

  • 批准号:
    8169329
  • 负责人:
  • 金额:
    $ 0.7万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
  • 财政年份:
    2010
  • 资助国家:
    美国
  • 起止时间:
    2010-04-01 至 2011-03-31
  • 项目状态:
    已结题

项目摘要

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Ubiquitylation regulates a variety of processes, including DNA repair, signal transduction, cell cycle progression, endocytosis and protein degradation, amongst others, and has been implicated in disease. The substrate specificity of the ubiquitylation system is carried out by the E3 protein ligases, which belong to two major families: the RING E3 ligases and the HECT E3 ligases. The HECT E3 ligases each contain an approximately 350 amino acid C-terminal catalytic domain with a conserved active site cysteine that forms a thiol-intermediate with ubiquitin, transferring it from an E2 ligase to the protein substrate. The highly variable N-terminal regions of the HECT E3s interact with specific protein substrates while the catalytic domain interacts with its cognate E2 and carries out the catalytic reaction. A variety of domains (WW domain, C2 domain, armadillo like-repeats, BH3, UBA, amongst others) have been observed in the N-terminus of the HECT domain proteins and these have been used to further classify these proteins. Unlike the HECT E3 ligases, the RING E3 ligases do not directly carry out the transfer of ubiquitin to substrate, but instead bring together the activated E2 and its substrate thus allowing catalysis to occur. We propose to determine the high-resolution structures of human E3 ligases and their complexes with cognate E2s, substrates and regulating factors in order to further elucidate their catalytic mechanisms, specificity and regulation. As part of the Structural Genomics Consortium, we have the capability to use high-throughput techniques to express and purify proteins, crystallize and characterize these crystals. However we require the brilliant X-rays available at the APS in order to collect data from weakly diffracting crystals and to collect anomalous data from heavy-atom derivatives.
这个子项目是众多研究子项目之一

项目成果

期刊论文数量(0)
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科研奖励数量(0)
会议论文数量(0)
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Alexei Bochkarev其他文献

Alexei Bochkarev的其他文献

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{{ truncateString('Alexei Bochkarev', 18)}}的其他基金

SGC TORONTO: CANADIAN MEDICAL PROTEIN-STRUCTURE HUNT
SGC 多伦多:加拿大医学蛋白质结构搜寻
  • 批准号:
    7955548
  • 财政年份:
    2009
  • 资助金额:
    $ 0.7万
  • 项目类别:
SGC TORONTO: CANADIAN MEDICAL PROTEIN-STRUCTURE HUNT
SGC 多伦多:加拿大医学蛋白质结构搜寻
  • 批准号:
    7721297
  • 财政年份:
    2008
  • 资助金额:
    $ 0.7万
  • 项目类别:

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