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

被引:6
作者
Yun, Hyosuk [1 ]
Kim, Eun-Hee [2 ]
Lee, Chul Won [1 ]
机构
[1] Chonnam Natl Univ, Dept Chem, 77 Yongbong Ro, Gwangju 61186, South Korea
[2] Korea Basic Sci Inst, Prot Struct Grp, Ochang 28119, South Korea
基金
新加坡国家研究基金会;
关键词
NMR resonance assignment; Periostin; Extracellular matrix; FAS1; domain; NMR-SPECTROSCOPY; EXPRESSION; CELL; SPECTRA; PROTON; FAMILY; GROWTH; BETA;
D O I
10.1007/s12104-017-9786-z
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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-1-N-15 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.
引用
收藏
页码:95 / 98
页数:4
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