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dc.contributor.authorLee, Erinna F-
dc.contributor.authorPerugini, Matthew A-
dc.contributor.authorPettikiriarachchi, Anne-
dc.contributor.authorEvangelista, Marco-
dc.contributor.authorKeizer, David W-
dc.contributor.authorYao, Shenggen-
dc.contributor.authorFairlie, W Douglas-
dc.identifier.citationAutophagy 2016; 12(3): 460-471-
dc.description.abstractBECN1/Beclin 1 has a critical role in the early stages of autophagosome formation. Recently, structures of its central and C-terminal domains were reported, however, little structural information is available on the N-terminal domain, comprising a third of the protein. This lack of structural information largely stems from the inability to produce this region in a purified form. Here, we describe the expression and purification of the N-terminal domain of BECN1 (residues 1 to 150) and detailed biophysical characterization, including NMR spectroscopy. Combined, our studies demonstrated at the atomic level that the BECN1 N-terminal domain is intrinsically disordered, and apart from the BH3 subdomain, remains disordered following interaction with a binding partner, BCL2L1/BCL-XL. In addition, the BH3 domain α-helix induced upon interaction with BCL2L1 reverts to a disordered state when the complex is dissociated by exposure to a competitive inhibitor. No significant interactions between N- and C-terminal domains were detected.-
dc.subjectBH3 domain-
dc.subjectBeclin 1-
dc.subjectintrinsically disordered protein; nuclear magnetic resonance-
dc.titleThe BECN1 N-terminal domain is intrinsically disordered.-
dc.typeJournal Article-
dc.identifier.affiliationThe Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia-
dc.identifier.affiliationDepartment of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia-
dc.identifier.affiliationOlivia Newton-John Cancer Research Institute, Heidelberg, Victoria, Australia-
dc.identifier.affiliationSchool of Cancer Medicine, La Trobe University, Melbourne, Victoria, Australia-
dc.identifier.affiliationBio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria, Australia-
dc.identifier.affiliationDepartment of Chemistry and Physics, La Trobe Institute for Molecular Science, Melbourne, Victoria, Australia-
dc.type.austinJournal Article-
dc.type.austinResearch Support, Non-U.S. Gov't-
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
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