Mapping the interaction site of prion protein and Sho

作者：Wan Jiayu; Hao Zhu; Xu Ming; Wang Xiong; Wu Songbo; Song Bocui; Liu Wensen; Li Jiping; Meng Keying; Li Zhongyi; Gao Hongwei^*

来源：Molecular Biology Reports, 2010, 37(5): 2295-2300.

DOI：10.1007/s11033-009-9722-0

• Prion protein
• Sho
• Yeast two-hybrid
• Surface plasmon resonance
• Co-immunoprecipitation
• Interaction

The cellular prion protein (PrP(C)) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP(C) remains unclear. Sho (Shadoo, shadow of prion protein) and PrP(C) have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon

• 出版日期2010-6
• 单位中国人民解放军军事医学科学院