학술논문
Structures of cGMP-dependent protein kinase (PKG) Ialpha leucine zippers reveal an interchain disulfide bond important for dimer stability
Document Type
Report
Author
Source
Biochemistry. July 28, 2015, Vol. 54 Issue 29, 4419-4422
Subject
Language
English
ISSN
0006-2960
Abstract
The article discusses the role of cGMP-dependent protein kinase (PKG) Ialpha in regulating smooth muscle tone and vasorelaxation. Crystal structures of the PKG Ialpha wild-type (WT) leucine zipper (LZ) and C42L LZ were determined for understanding the molecular details of the PKG Ialpha LZ and C42uC42E disulfide bond. It was found that the C42uC42E bond stabilized PKG Ialpha, while the C42L mutant structurally mimicked oxidized WT LZ.