Structural highlights
Function
[POSTN_HUMAN] Induces cell attachment and spreading and plays a role in cell adhesion (PubMed:12235007). Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity).[UniProtKB:Q62009][1]
Publication Abstract from PubMed
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.
(1)H, (13)C, and (15)N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins.,Yun H, Kim EH, Lee CW Biomol NMR Assign. 2017 Oct 31. pii: 10.1007/s12104-017-9786-z. doi:, 10.1007/s12104-017-9786-z. PMID:29086898[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gillan L, Matei D, Fishman DA, Gerbin CS, Karlan BY, Chang DD. Periostin secreted by epithelial ovarian carcinoma is a ligand for alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility. Cancer Res. 2002 Sep 15;62(18):5358-64. PMID:12235007
- ↑ Yun H, Kim EH, Lee CW. (1)H, (13)C, and (15)N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins. Biomol NMR Assign. 2017 Oct 31. pii: 10.1007/s12104-017-9786-z. doi:, 10.1007/s12104-017-9786-z. PMID:29086898 doi:http://dx.doi.org/10.1007/s12104-017-9786-z
