1H, 15N, 13C resonance assignment of human osteopontin

被引：0
|
作者：
Gerald Platzer
Szymon Żerko
Saurabh Saxena
Wiktor Koźmiński
Robert Konrat
机构：
[1] University of Vienna,Max F. Perutz Laboratories, Department of Computational and Structural Biology
[2] University of Warsaw,Faculty of Chemistry, Biological and Chemical Research Centre
来源：
Biomolecular NMR Assignments | 2015年 / 9卷
关键词：
Osteopontin; Intrinsically disordered protein; Extracellular matrix; Biomineralization;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
Osteopontin (OPN) is a 33.7 kDa intrinsically disordered protein and a member of the SIBLING family of proteins. OPN is bearing a signal peptide for secretion into the extracellular space, where it exerts its main physiological function, the control of calcium biomineralization. It is often involved in tumorigenic processes influencing proliferation, migration and survival, as well as the adhesive properties of cancer cells via CD44 and integrin signaling pathways. Here we report the nearly complete NMR chemical shift assignment of recombinant human osteopontin.
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页码：289 / 292
页数：3
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