Yun Hyosuk, Kim Eun-Hee, Lee Chul Won
Department of Chemistry, Chonnam National University, 77 Yongbong-ro, Buk-gu, Gwangju, 61186, Republic of Korea.
Protein Structure Group, Korea Basic Science Institute, Ochang, 28119, Republic of Korea.
Biomol NMR Assign. 2018 Apr;12(1):95-98. doi: 10.1007/s12104-017-9786-z. Epub 2017 Oct 31.
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 H-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.
骨膜蛋白是一种细胞外基质蛋白，由成纤维细胞分泌，在多种癌症中过度表达。人骨膜蛋白的四个内部重复的成束蛋白1（FAS1）结构域通过与细胞表面整合素相互作用，在促进肿瘤转移和进展中发挥关键作用。在人骨膜蛋白的四个FAS1结构域中，第四个FAS1结构域（FAS1-IV）被制备用于核磁共振（NMR）研究，因为只有FAS1-IV高度可溶，并显示出分散良好的二维氢-氮异核单量子相干（2D H-N HSQC）谱。在此，我们报告了几乎完整的主链和侧链共振归属以及FAS1-IV结构域的二级结构分析，作为确定人骨膜蛋白FAS1-IV结构的第一步。
