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Expression and Preparation of Periostin FAS1 Domains for NMR Structure Determination

  • Yun, Hyosuk (Department of Chemistry, Chonnam National University) ;
  • Kim, Jae Il (Department of Life Science, Gwangju Institute of Science and Technology) ;
  • Lee, Chul Won (Department of Chemistry, Chonnam National University)
  • Received : 2016.01.03
  • Accepted : 2016.02.19
  • Published : 2016.03.20

Abstract

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.

Keywords

References

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Cited by

  1. 1H, 13C, and 15N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins pp.1874-270X, 2017, https://doi.org/10.1007/s12104-017-9786-z