Molecular structure and regulate mechanisms of the peptidyl prolyl cis/trans isomerase Pin1
- VernacularTitle:肽基脯氨酰顺反异构酶Pin1的分子结构与调节机制
- Author:
Qiang CAO
;
Jun GUO
- Publication Type:Journal Article
- Keywords:
Pin1;
Post-translational modifications;
Substrates;
Regulatory mechanism
- From:
Journal of Medical Postgraduates
2003;0(05):-
- CountryChina
- Language:Chinese
-
Abstract:
The peptidyl prolyl cis/trans isomerase Pin1 specifically binds phosphorylated Ser/Thr-Pro protein motifs and catalyzes the cis/trans isomerization of the peptide bond,changes the conformation and influences the stability and activity of the substrates.To date,a subset of proteins has been identified as substrates for Pin1.Pin1 interacts with its substrates and plays crucial roles in cell cycle,neural pathology and immune response.Accumulating studies have revealed that Pin1 isomerase activity is regulated by its post-translational modifications,including phosphorylation and oxidation.Over-expression or regulative imbalance of Pin1 plays an important role in the pathogenesis and therapeutics of human diseases such as cancer and AD.
