Structure and function of the human parvulins Pin1 and Par14/17
Author:
Matena Anja1, Rehic Edisa1, Hönig Dana1, Kamba Bianca1, Bayer Peter1
Affiliation:
1. Structural and Medicinal Biochemistry, Center for Medical Biotechnology (ZMB), Faculty of Biology , University of Duisburg-Essen , Universitätsstr. 2 , D-45117 Essen , Germany
Abstract
Abstract
Parvulins belong to the family of peptidyl-prolyl cis/trans isomerases (PPIases) assisting in protein folding and in regulating the function of a broad variety of proteins in all branches of life. The human representatives Pin1 and Par14/17 are directly involved in processes influencing cellular maintenance and cell fate decisions such as cell-cycle progression, metabolic pathways and ribosome biogenesis. This review on human parvulins summarizes the current knowledge of these enzymes and intends to oppose the well-studied Pin1 to its less well-examined homolog human Par14/17 with respect to structure, catalytic and cellular function.
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Reference223 articles.
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