Key result
Preparation of Periostin FAS1 domains in E. coli revealed that the single FAS1-IV domain is highly soluble and suitable for three-dimensional structure determination using NMR spectroscopy.
The FAS1-IV domain of periostin is highly soluble and suitable for 3D structure determination using NMR spectroscopy.
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Facilitates periostin NMR studies; leaves open any role in cardiac remodeling or clinical translation.
Periostin, a component of extracellular matrix (ECM) protein, is produced and secreted by the fibroblasts that are involved in chronic allergic inflammation diseases and various types of human cancers. Periostin protein is composed of multiple domains including four FAS1 domains which play important roles in cell adhesion and tumor metastasis by interacting with integrins. In spite of their important biological role, the structural information of periosin FAS1 domains was not revealed yet. Recently we systemically prepared various constructs of the FAS1 domains and tried to express them in E. coli. Of them, only single FAS1-II and -IV domains were highly soluble. Circular dichroism (CD) and nuclear magnetic resonance (NMR) studies revealed that the FAS1-IV domain might be suitable for three-dimensional structure determination using NMR spectroscopy.
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Yun et al. (2016) studied this question. Periostin FAS1 domains was evaluated. Preparation of Periostin FAS1 domains in E. coli revealed that the single FAS1-IV domain is highly soluble and suitable for three-dimensional structure determination using NMR spectroscopy.
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