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首页> 外文期刊>Biotechnology Progress >Molecular Dynamics Simulations to Investigate the Effects of Zinc Ions on the Structural Stability of the c-Cbl RING Domain
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Molecular Dynamics Simulations to Investigate the Effects of Zinc Ions on the Structural Stability of the c-Cbl RING Domain

机译：分子动力学模拟，以研究锌离子对c-Cbl RING结构域的结构稳定性的影响

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In eukaryotic cells,ubiquitylation of proteins plays a critical role in regulating diverse cell processes by the ubiquitin activating enzyme(E1),ubiquitin-conjugating enzyme(E2),and ubiquitin protein ligase(E3).E3 is the key component that confers specificity to ubiquitylation and directs the conjugation of ubiquitin to a specific target protein.RING domains are small structured protein domains that require the coordination of zinc ions for a stable tertiary fold and some of them are involved in the E3 family.In this study,we reported the detailed relationships between the two zinc ions and the structural stability of the c-Cbl RING domain by molecular dynamics simulations.Our results show that these two zinc ions play an important role in maintaining both the secondary and tertiary structural stabilities of the c-Cbl RING domain.Our results also reveal that the secondary structural stability of the c-Cbl RING domain is mainly determined by the hydrogen-bonding networks in or near the two zinc ion binding sites.Our results further demonstrate that zinc ion binding site 2 is more structurally stable than site 1.
机译：在真核细胞中，蛋白质的泛素化作用通过泛素激活酶（E1），泛素结合酶（E2）和泛素蛋白连接酶（E3）在调节各种细胞过程中起关键作用。E3是赋予特异性的关键成分环结构域是小的结构化蛋白结构域，需要锌离子的配合才能稳定地形成第三级折叠，其中一些涉及E3家族。在这项研究中，我们报道了通过分子动力学模拟详细了解了两个锌离子与c-Cbl RING结构域之间结构关系。我们的结果表明，这两个锌离子在维持c-Cbl RING的二级和三级结构稳定性方面都起着重要作用我们的结果还揭示了c-Cbl RING域的二级结构稳定性主要取决于氢键网络中或附近的氢键网络。两个锌离子结合位点。我们的结果进一步证明锌离子结合位点2在结构上比位点1更稳定。

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