Molecular dynamics of zinc-finger ubiquitin bindin

更新时间:2023-07-25 14:06:12 阅读: 评论:0

Molecular dynamics of zinc-finger ubiquitin binding domains: a comparative study of histone deacetyla 6 and ubiquitin-specific protea 5制川乌的功效与作用
难忘的眼神作文期刊名称: Journal of Biomolecular Structure & Dynamics
风险管控制度
乔布斯和比尔盖茨作者: Carolina dos Santos Passos,Claudia A. Simes-Pires,Pierre-Alain
Carrupt,Alessandra Nurisso
年份: 2015年
期号: 第12期
关键词: HDAC6;USP5;zinc-finger ubiquitin binding domain;ubiquitin;molecular担当责任
dynamics
摘要:HDAC6 is a unique cytoplasmic histone deacetyla characterized by two deacetyla domains, and by a zinc-finger ubiquitin binding domain (ZnF-UBP) able
相思风雨中吉他谱
to recognize ubiquitin (Ub). The latter has recently been demonstrated to be involved in the progression of neurodegenerative dias and in mediating infection by the influenza A virus. Nowadays, understanding the dynamic and energetic features of HDAC6 ZnF-UBP-Ub recognition is considered as a crucial step for the conception of HDAC6 potential modulators. In this study, the atomic,
垃圾英文骂人lesolvent-related, and thermodynamic features behind HDAC6 ZnF-UBP-Ub recognition have been analyzed through molecular dynamics simulations. The behavior was then compared to the prototypical ZnF-UBP from ubiquitin-specific protea 5 (USP5) in order to spot relevant differences uful for
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