THE STRUCTURAL AND FUNCTIONAL-ORGANIZATION OF INTRAMOLECULAR CHAPERONES - THE N-TERMINAL PROPEPTIDES WHICH MEDIATE PROTEIN-FOLDING

被引：51

作者：

SHINDE, U

INOUYE, M

机构：

[1] Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, N.J. 08854

来源：

JOURNAL OF BIOCHEMISTRY | 1994年 / 115卷 / 04期

关键词：

INTRAMOLECULAR CHAPERONE; PROPEPTIDES; PROTEIN FOLDING; SUBTILISIN;

D O I：

10.1093/oxfordjournals.jbchem.a124386

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A large number of prokaryotic as well as eukaryotic proteins are produced with amino terminal propeptides. These amino-terminal extensions are essential for mediating proper folding of their corresponding proteins and are also termed as intramolecular chaperones. Though these propeptides are highly specific and unique in their function, several common features have been identified and indicate that the overall mechanism by which they function may be very similar.

引用

页码：629 / 636

页数：8

共 32 条

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