蛋白酶体结构和功能研究进展  

Recent Advances in the Structure and Functions of the Proteasome

作　　者：彭睿[1,2] 秦浚川[1,2] 宋晓龄 

机构地区：[1]南京大学生物化学系医药生物技术国家重点实验室 [2]美国Texas大学西南医学中心

出　　处：《生物化学与生物物理进展》1998年第3期235-238,共4页Progress In Biochemistry and Biophysics

摘　　要：蛋白酶体是真核细胞内依赖ＡＴＰ的蛋白质水解途径的重要成分，负责大多数细胞内蛋白质的降解．２０Ｓ蛋白酶体有多种肽酶活性，其活性位点为Ｔｈｒ．１９Ｓ复合物与２０Ｓ蛋白酶体结合成为２６Ｓ复合物，能降解泛素化蛋白．近几年来，蛋白酶体的分子组成、亚基、生化机理、胞内功能等方面的研究取得了明显进展．The proteasome is an essential component of the ATPdependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. The 20 S proteasome whose active site is a threonine,contains multiple peptidase activities. PA700 cappes the 20 S proteasome to form the 26 S complex, by which ubiquitinated proteins are degraded. Advances have been achieved recently in the research about the molecular organization of the 20 S and 26 S particles,their subunits,their intracellular functions and biochemical mechanisms.

关 键 词：蛋白酶体 结构 功能 活化因子 

分 类 号：Q556[生物学—生物化学]