1H, 13C, and 15N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins
- 125 Downloads
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.
KeywordsNMR resonance assignment Periostin Extracellular matrix FAS1 domain
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).
- Bruder SP, Ricalton NS, Boynton RE, Connolly TJ, Jaiswal N, Zaia J, Barry FP (1998) Mesenchymal stem cell surface antigen SB-10 corresponds to activated leukocyte cell adhesion molecule and is involved in osteogenic differentiation. J Bone Min Res 13:655–663. doi: 10.1359/jbmr.19126.96.36.1995 CrossRefGoogle Scholar
- Horiuchi K et al (1999) Identification and characterization of a novel protein, periostin, with restricted expression to periosteum and periodontal ligament and increased expression by transforming growth factor beta. J Bone Min Res 14:1239–1249. doi: 10.1359/jbmr.19188.8.131.529 CrossRefGoogle Scholar
- Marion D, Driscoll PC, Kay LE, Wingfield PT, Bax A, Gronenborn AM, Clore GM (1989) Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. Biochemistry 28:6150–6156CrossRefGoogle Scholar