Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2009.04.024
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dc.titleNMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis
dc.contributor.authorLiu, J.
dc.contributor.authorSong, J.
dc.contributor.authorZhu, W.
dc.contributor.authorQin, H.
dc.date.accessioned2011-11-29T06:10:34Z
dc.date.available2011-11-29T06:10:34Z
dc.date.issued2009
dc.identifier.citationLiu, J., Song, J., Zhu, W., Qin, H. (2009). 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 383 (4) : 433-439. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2009.04.024
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/28881
dc.description.abstractRTN3 can recruit Fas-associated death domain (FADD), thus initiating the ER-stress activated apoptosis. It also interacts with the β-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. Nevertheless, the C-terminus contains two short helix-populated regions. (2) The unstructured hRTN3 C-terminus can bind to hFADD as shown by ITC. Further NMR investigation successfully identified the binding involved hRTN3 residues. (3) Although upon hRTN3-binding, the perturbed hFADD residues were distributed over the whole sequence, the majority of the significantly perturbed are over its death effector domain, very different from the previously observed binding mode for FADD. This study also implies a possible linkage between Alzheimer's disease and ER-stress activated apoptosis. © 2009 Elsevier Inc. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bbrc.2009.04.024
dc.sourceScopus
dc.subjectApoptosis
dc.subjectCircular dichroism (CD)
dc.subjectEndoplasmic reticulum (ER)
dc.subjectFas-associated death domain (FADD)
dc.subjectIntrinsically unstructured protein
dc.subjectIsothermal titration calorimetry (ITC)
dc.subjectNMR spectroscopy
dc.subjectReticulon 3 (RTN3)
dc.subjectRTN4/Nogo
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.bbrc.2009.04.024
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume383
dc.description.issue4
dc.description.page433-439
dc.description.codenBBRCA
dc.identifier.isiut000266227000011
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