摘要
PCID2和DSS1是TREX2复合体中的成分,DSS1作为子复合体之间的粘合剂在复合体中主要与PCID2结合.研究发现,DSS1在复合体中起稳定PCID2的作用.利用分子动力学模拟研究无序蛋白DSS1与PCID2的相互作用,结果表明:未结合DSS1的单体PCID2蛋白构象不稳定,与DSS1结合后的PCID2蛋白构象明显变得更稳定,特别是与DSS1结合处的构象,与实验得出的结论一致.研究DSS1对PCID2的作用,不仅可以为了解PCI蛋白提供分子基础,也为深入了解TREX复合体在核酸输出中的功能提供帮助.
PCID2 and DSS1 are component of the TREX-2 complex, and as a multitasking organizer of protein complexes DSS1 binds primarily to PCID2. DSS1 has been suggested stabilizing the conformation of PCID2. Molecular dynamics （MD） simulations were performed to study the interactions between DSS1 and PCID2. The results indicate that the monomeric PCID2 protein without DSS1 is unstable, and DSS1 in the binding domain maintain can stable the conformation of PCID2. These results are in good consistence with experimental data. This work doesn＇t only provide a molecular basis for understanding the PCI-protein, but also provides insight into the function of TREX--2 complex in coupling transcription and processing, with mRNA export.
出处
《德州学院学报》
2014年第2期1-5,共5页
Journal of Dezhou University
基金
山东省自然科学基金资助项目(2009ZRA14028)
关键词
PCID2蛋白
分子动力学模拟
构象变化
PCID2 protein
molecular dynamics simulation
conformational changes
