MULTIPLE FUNCTIONS OF PRO-PARTS OF ASPARTIC PROTEINASE ZYMOGENS

被引:86
作者
KOELSCH, G
MARES, M
METCALF, P
FUSEK, M
机构
[1] OKLAHOMA MED RES FDN, OKLAHOMA CITY, OK 73104 USA
[2] UNIV OKLAHOMA, HLTH SCI CTR, OKLAHOMA CITY, OK 73104 USA
[3] ACAD SCI CZECH REPUBL, INST ORGAN CHEM & BIOCHEM, CR-16610 PRAGUE, CZECH REPUBLIC
[4] EUROPEAN MOLEC BIOL LAB, W-6900 HEIDELBERG, GERMANY
来源
FEBS LETTERS | 1994年 / 343卷 / 01期
关键词
ASPARTIC PROTEINASE; CHAPERON; FOLDING; PRO-PART; PROTEIN STRUCTURE; TARGETING;
D O I
10.1016/0014-5793(94)80596-2
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
The importance of aspartic proteinases in human pathophysiology continues to initiate extensive research. With burgeoning information on their biological functions and structures, the traditional view of the role of activation peptides of aspartic proteinases solely as inhibitors of the active site is changing. These peptide segments, or pro-parts, are deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. Consequently, the primary structures of pro-parts reflect these functions. We discuss guidelines for formation of hypotheses derived from comparing the physiological function of aspartic proteinases and sequences of their pro-parts.
引用
收藏
页码:6 / 10
页数:5
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