Article
NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis.
Biochemical and biophysical research communications - 12 Jun 2009
Liu Jingxian, Zhu Wanlong, Qin Haina, Song Jianxing
Abstract excerpt
RTN3 can recruit Fas-associated death domain (FADD), thus initiating the ER-stress activated apoptosis. It also interacts with the beta-secretase and its aggregation is critically associated with Alzheimer's disease. Here, we first investigated the solution conformation of hRTN3, subsequently characterized its binding with hFADD. The results reveal: (1) both hRTN3 N- and C-termini are intrinsically unstructured....
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