Structures and functions of chaperones and chaperonins - (Review)

被引：13

作者：

Evstigneeva, ZG ^{[1
]}

Solov'eva, NA ^{[1
]}

Sidel'nikova, LI ^{[1
]}

机构：

[1] Russian Acad Sci, Bach Inst Biochem, Moscow 117071, Russia

来源：

APPLIED BIOCHEMISTRY AND MICROBIOLOGY | 2001年 / 37卷 / 01期

关键词：

D O I：

10.1023/A:1002835921817

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Folding and assembling of newly synthesized proteins is directed and effected by a group of relatively recently discovered proteins called molecular chaperones. These proteins not only control the assembling of native structures; they also remodel protein molecules that have wrong conformations. All molecular chaperones perform the same function, but structurally they are divided into groups of chaperones and chaperonins. These proteins are highly conserved in evolution and display an ATPase activity. Certain known chaperones and chaperonins are shown in the table, and their structures and mechanisms of action are described.

引用

页码：1 / 13

页数：13

共 73 条

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