摘要
兔成年骨骼肌型肌浆网-内质网钙离子转运ATP酶(adult skeletal sarco-endoplasmic reticulum Ca2+-transporting ATPase,SERCA1a)是结构与功能研究得最好的膜蛋白之一,可利用ATP水解释放的能量,逆浓度梯度将胞浆内钙离子转运入内质网钙库,保证骨骼肌收缩舒张的正常进行。近年来,X-射线晶体衍射分析获得的数十个高分辨率晶体结构提供的结构信息,结合生化检测获得的重要氨基酸残基突变对SERCA1a反应循环动力学的影响,使对SERCA1a分子构象的周期性变化以及SERCA1a如何转运钙离子、自身磷酸化与去磷酸化等重要过程的理解更加清晰且深入。SERCA1a结构与功能的研究进展对P型离子转运ATP酶的基础与应用研究具有指导意义与促进作用。
The rabbit adult skeletal sarco-endoplasmic reticulum Ca^2＋-transPorting ATPase SERCA1 a is one of the structurally and functionally best-studied membrane proteins. SERCA1 a proteins utilize energy from ATP hydrolysis to transport calcium ions retrograde from cytosol into the endoplasmic reticulum calcium store, by which contraction and relaxation of skeletal muscle may go on normally. In recent years, fine structural information provided by X-ray crystallography, combining with kinetic changes of the SERCA1 a reaction cycle induced by single mutations of some critical amino acid residues, clarifies or deepens the understanding about questions such as the periodic change of SERCA1 a conformations, how SERCA1 a transPorts calcium ions, how SERCA1 a auto-phosphorylates and dephosphorylates, and so on. The progress of structural and functional studies on SERCA1 a may guide and propel the theoretical or applicable research of P-type ion transPort ATPases.
出处
《生命的化学》
CAS
CSCD
2015年第6期703-708,共6页
Chemistry of Life
基金
辽宁省科学技术厅暨辽宁省财政厅科学技术计划(2009225008-9)
