Multiple functions of pro‐parts of aspartic proteinase zymogens

FEBS Letters

Metcalf, Peter³  Fusek, Martin²  Koelsch, Gerald²  Mareš, Michael¹ 

[1] Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Prague, CZ 16610, Czech Republic;Oklahoma Medical Research Foundation and University of Oklahoma Health Sciences Center, 82S N.E. 13th Street, Oklahoma City, OK 73104, USA;European Molecular Biology Laboratory, Heidelberg, D-6900, Germany

关键词: Aspartic proteinase;    Chaperon;    Folding;    Pro-part;    Protein structure;    Targeting;   

DOI  :  10.1016/0014-5793(94)80596-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown