5WT7

1H,13C, and 15N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins.

(2018) Biomol NMR Assign 12: 95-98

• PubMed: 29086898 Search on PubMed
• DOI: https://doi.org/10.1007/s12104-017-9786-z
• Primary Citation of Related Structures:  
  5WT7


• PubMed Abstract: 
  

  Periostin, an extracellular matrix protein, is secreted by fibroblasts and is overexpressed in various types of cancers. The four internal repeat fasciclin 1 (FAS1) domains of human periostin play crucial roles in promoting tumor metastasis and progression via interaction with cell surface integrins. Among four FAS1 domains of human periostin, the fourth FAS1 domain (FAS1-IV) was prepared for NMR study, since only FAS1-IV was highly soluble, and showed a well-dispersed 2D ¹ H- ¹⁵ N HSQC spectrum. Here, we report nearly complete backbone and side chain resonance assignments and a secondary structural analysis of the FAS1-IV domain as first steps toward the structure determination of FAS1-IV of human periostin.

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Organizational Affiliation: 

Department of Chemistry, Chonnam National University, 77 Yongbong-ro, Buk-gu, Gwangju, 61186, Republic of Korea.