Structural variability of the ubiquitin specific protease DUSP-UBL double domains
Structural variability of the ubiquitin specific protease DUSP-UBL double domains
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DOI：
10.1016/j.febslet.2011.09.040
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发表时间：
2011-11-04
期刊：
影响因子：
3.5
通讯作者：
Barsukov, Igor L.
中科院分区：
文献类型：
--
作者：
Elliott, Paul R.;Liu, Han;Barsukov, Igor L.
USP 4、11和15是去泛素化酶的泛素特异性蛋白酶（USP）家族的三个密切相关的旁系同源物。这些蛋白质中的DUSP结构域和UBL结构域并置，这可以提供赋予特异性的功能单元。我们确定了单体和二聚体状态下USP 15 DUSP-UBL双结构域单元的结构。然后，我们对所有三个DUSP-UBL单元的结构和物理性质进行了比较分析。我们确定了决定组成结构域之间不同配置的结构特征，这反过来又可能影响各自的结合特性。蛋白质相互作用的结构总结：USP 15和USP 15通过分子筛结合（查看相互作用：1，2）USP 15和USP 15通过分子筛进行物理相互作用（查看相互作用）USP 4和USP 4通过分子筛结合（查看交互：1,2）USP 15和USP 15通过X射线散射结合（查看相互作用）USP 11和USP 11通过分子筛结合（查看相互作用）USP 4和USP 4通过核磁共振结合（查看相互作用）USP 15和USP 15通过X射线晶体学结合（查看相互作用）（C）2011欧洲生物化学学会联合会。由Elsevier B出版。V.保留所有权利。
USP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP) family of deubiquitinating enzymes. The DUSP domain and the UBL domain in these proteins are juxtaposed which may provide a functional unit conferring specificity. We determined the structures of the USP15 DUSP-UBL double domain unit in monomeric and dimeric states. We then conducted comparative analysis of the structural and physical properties of all three DUSP-UBL units. We identified structural features that dictate different dispositions between constituent domains, which in turn may influence respective binding properties.Structured summary of protein interactions:USP15 and USP15 bind by molecular sieving (View Interaction: 1, 2)USP15 and USP15 physically interact by molecular sieving (View interaction)USP4 and USP4 bind by molecular sieving (View Interaction: 1, 2)USP15 and USP15 bind by X ray scattering (View interaction)USP11 and USP11 bind by molecular sieving (View interaction)USP4 and USP4 bind by nuclear magnetic resonance (View interaction)USP15 and USP15 bind by X-ray crystallography (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.