The structure of phospholamban and its MD simulations  

作　　者：TANG Bei GONG Ke WANG JingFang LI YiXue WEI DongQing 

机构地区：[1]Department of Bioinformatics and Biostatistics, College of Life Science and Technology, Shanghai Jiao Tong University, Shanghai 200240, China [2]Bioinformatics Center, Key Laboratory of Systems Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai200031, China

出　　处：《Chinese Science Bulletin》2010年第16期1619-1624,共6页

基　　金：supported by the National Natural Science Foundation of China (20773085 and 30870476);National High-Tech Research and Devel-opment Program of China (2007AA02Z333);Major Chinese National Funding of New Drug Discovery for the Integrated Platform

摘　　要：Phospholamban is an important protein with responsibility for regulating the activity of the sarcoplasmic reticulum Ca2+ pump through reversible phosphorylation.And its three-dimensional structure in living cell has been a focus of attention.In the current case, we summarized the investigations on phospholamban structure, and on this base, employed long time-scale molecular dy-namics simulations to study its structure systematically.The first 22 residues from one chain of phospholamban in bellflower structure determined by NMR experiments, together with its phosphorylation at position 16 and mutation at position 9 were picked up as three different systems.By molecular dynamics simulations of 10 ns in the explicit solution surroundings, it was found that the 3–15 residues of the original structure retained their helix structures, while the phosphorylation and mutation had less probability to form helix structures.These structural changes might result in inhibition decrease to the sarcoplasmic reticulum Ca2+ pump, which is in accordance with previous experimental results.Phospholamban is an important protein with responsibility for regulating the activity of the sarcoplasmic reticulum Ca^2＋ pump through reversible phosphorylation. And its three-dimensional structure in living cell has been a focus of attention. In the current case, we summarized the investigations on phospholamban structure, and on this base, employed long time-scale molecular dynamics simulations to study its structure systematically. The first 22 residues from one chain of phospholamban in bellflower structure determined by NMR experiments, together with its phosphorylation at position 16 and mutation at position 9 were picked up as three different systems. By molecular dynamics simulations of 10 ns in the explicit solution surroundings, it was found that the 3-15 residues of the original structure retained their helix structures, while the phosphorylation and mutation had less probability to form helix structures. These structural changes might result in inhibition decrease to the sarcoplasmic reticulum Ca^2＋ pump, which is in accordance with previous experimental results.

关 键 词：分子动力学模拟 可逆磷酸化 三维结构 结构系统 实验确定 螺旋结构 基因突变 蛋白结构 

分 类 号：Q51[生物学—生物化学]