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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of human TSG101 UEV domain.
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Structure of human TSG101 UEV domain.

机译：结构的人类TSG101 UEV域。

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摘要

The UEV domain of the TSG101 protein functions in the vacuolar protein-sorting pathway and in the budding process of HIV-1 and other retroviruses by recognizing ubiquitin in proteins tagged for degradation and short sequences in viral proteins containing an essential and well conserved PTAP motif, respectively. A deep understanding of these interactions is key to the rational design of much-needed novel antivirals. Here, the crystal structure of the TSG101 UEV domain (TSG101-UEV) is presented. TSG101-UEV was crystallized in the presence of PEG 4000 and ammonium sulfate. Under these conditions, crystals were obtained in space group R3, with unit-cell parameters a = b = 97.9, c = 110.6 A, alpha = beta = 90, gamma = 120 degrees . Phases were solved by molecular replacement and the crystal structure of TSG101-UEV was refined to an R factor of 18.8% at 2.2 A resolution. A comparison between the crystal structure and previously reported NMR structures has revealed significant differences in the conformation of one of the loops implicated in ubiquitin recognition. Also, the resulting structure has provided information about the presence of water molecules at the binding interface that could be of relevance for peptide recognition.
机译：UEV域TSG101蛋白质的功能空泡protein-sorting通路和初露头角的hiv - 1和其它逆转录病毒的过程通过识别蛋白质的泛素标记在病毒蛋白质退化和短序列包含一个基本和守恒PTAP分别为主题。这些交互是理性设计的关键急需的新型抗病毒药物。晶体结构的TSG101 UEV域(TSG101-UEV)。结晶的4000和挂钩硫酸铵。在空间群R3晶体得到,晶胞参数a = b = 97.9, c = 110.6,α=β= 90,γ= 120度。通过分子置换和解决晶体结构TSG101-UEV精炼的分辨率2.2 R因子的18.8%。晶体结构和之间的比较之前报道揭示了NMR结构显著差异的构象循环与泛素之一识别。水的存在提供信息分子可以在绑定接口相关的肽识别。

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