p53蛋白质Gly249和Ser249替换型三维结构的分子动力学研究

利用p53蛋白质核心区晶体结构作分子动力学发现，除了生化方面的稳定性之外，该区还具有分子力学上的高度稳定性.在此基础上作的R249残基替换分子动力学研究显示，p53蛋白质核心区249位点精氨酸被其他残基替换后能引起p53蛋白质核心区L2、L3结构域间的密切联系趋于松散，正常的空间构象发生改变并使整个核心区结构稳定性受到破坏.这一研究从三维结构变化上，直观地解释了R249残基替换造成的p53蛋白质免疫和生化特性改变的结构机制.

Molecular Dynamics Research of G249 and S249 Substitutions of p53 Protein

The molecular dynamics research of the core domain of p53 protein crystal structure shows that besides the stability in biochemistry this domain also shows a high stability in molecular mechanics. Based on that work, the residue R249 was substituted with amino acids Gly and Ser respectively, and molecular dynamics researches were performed separately. The results show that these substitutions cause a relax tendency between loop2 and 3 domains, leading to an alteration of the whole conformation of p53 core domain and ruining its stability. The results visually explains the mechanism of p53 changes in immunological and biochemical reactions, which are caused by 249 residue substitutions from 3-D structure variations.