Biotechnology Center (BIOTEC), Technische Universität Dresden, Dresden, Germany.
Proteomics. 2010 Dec;10(23):4186-95. doi: 10.1002/pmic.201000283.
Set1C is a histone methyltransferase playing an important role in yeast gene regulation. Modeling the structure of this eight-subunit protein complex is an important open problem to further elucidate its functional mechanism. Recently, there has been progress in modeling of larger complexes using constraints to restrict the combinatorial explosion in binary docking of subunits. Here, we model the subunits of Set1C and develop a constraint-based docking approach, which uses high-quality protein interaction as well as functional data to guide and constrain the combinatorial assembly procedure. We obtained 22 final models. The core complex consisting of the subunits Set1, Bre2, Sdc1 and Swd2 is conformationally conserved in over half of the models, thus, giving high confidence. We characterize these high-confidence and the lower confidence interfaces and discuss implications for the function of Set1C.
Set1C 是一种组蛋白甲基转移酶，在酵母基因调控中发挥着重要作用。对这个由八个亚基组成的蛋白质复合物的结构进行建模，是进一步阐明其功能机制的一个重要的开放性问题。最近，利用约束条件来限制亚基二进制对接的组合爆炸，在对更大的复合物进行建模方面取得了进展。在这里，我们对 Set1C 的亚基进行建模，并开发了一种基于约束的对接方法，该方法使用高质量的蛋白质相互作用以及功能数据来指导和限制组合组装过程。我们得到了 22 个最终模型。由 Set1、Bre2、Sdc1 和 Swd2 组成的核心复合物在超过一半的模型中构象保守，因此具有很高的可信度。我们对这些高可信度和低可信度的界面进行了特征描述，并讨论了它们对 Set1C 功能的影响。
