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 1H-15N 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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Acknowledgements
We would like to thank the Basic Science Research Institute at Ochang, Korea, for performing the high-field NMR experiments. This work was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science, and Technology of Korea (NRF-2013R1A1A2009419 to C.W.L).
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Yun, H., Kim, EH. & Lee, C.W. 1H, 13C, and 15N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins. Biomol NMR Assign 12, 95–98 (2018). https://doi.org/10.1007/s12104-017-9786-z
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DOI: https://doi.org/10.1007/s12104-017-9786-z