Nair S K, Burley S K
Department of Biochemistry and Center for Biophysics & Computational Biology, University of Illinois at Urbana-Champaign, 600 S. Mathews Avenue, Urbana, IL 61801, USA.
Curr Top Microbiol Immunol. 2006;302:123-43. doi: 10.1007/3-540-32952-8_5.
Recently determined structures of a number of Myc family proteins have provided significant insights into the molecular nature of complex assembly and DNA binding. These structures illuminate the details of specific interactions that govern the assembly of nucleoprotein complexes and, in doing so, raise more questions regarding Myc biology. In this review, we focus on the lessons provided by these structures toward understanding (1) interactions that govern transcriptional repression by Mad via the Sin3 pathway, (2) homodimerization of Max, (3) heterodimerization of Myc-Max and Mad-Max, and (4) DNA recognition by each of the Max-Max, Myc-Max, and Mad-Max dimers.
最近确定的一些Myc家族蛋白的结构，为深入了解复合物组装和DNA结合的分子本质提供了重要见解。这些结构阐明了控制核蛋白复合物组装的特定相互作用的细节，在此过程中，也引发了更多有关Myc生物学的问题。在本综述中，我们重点关注这些结构所提供的经验教训，以理解：（1）Mad通过Sin3途径进行转录抑制的相互作用；（2）Max的同二聚化；（3）Myc-Max和Mad-Max的异二聚化；以及（4）Max-Max、Myc-Max和Mad-Max二聚体各自对DNA的识别。
