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https://ahro.austin.org.au/austinjspui/handle/1/17644
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DC Field | Value | Language |
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dc.contributor.author | Lee, Erinna F | - |
dc.contributor.author | Perugini, Matthew A | - |
dc.contributor.author | Pettikiriarachchi, Anne | - |
dc.contributor.author | Evangelista, Marco | - |
dc.contributor.author | Keizer, David W | - |
dc.contributor.author | Yao, Shenggen | - |
dc.contributor.author | Fairlie, W Douglas | - |
dc.date.accessioned | 2018-05-02T23:36:37Z | - |
dc.date.available | 2018-05-02T23:36:37Z | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | Autophagy 2016; 12(3): 460-471 | - |
dc.identifier.uri | https://ahro.austin.org.au/austinjspui/handle/1/17644 | - |
dc.description.abstract | BECN1/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.language.iso | eng | - |
dc.subject | BCL2 | - |
dc.subject | BECN1 | - |
dc.subject | BH3 domain | - |
dc.subject | Beclin 1 | - |
dc.subject | autophagy | - |
dc.subject | intrinsically disordered protein; nuclear magnetic resonance | - |
dc.title | The BECN1 N-terminal domain is intrinsically disordered. | - |
dc.type | Journal Article | - |
dc.identifier.journaltitle | Autophagy | - |
dc.identifier.affiliation | The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia | - |
dc.identifier.affiliation | Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia | - |
dc.identifier.affiliation | Olivia Newton-John Cancer Research Institute, Heidelberg, Victoria, Australia | - |
dc.identifier.affiliation | School of Cancer Medicine, La Trobe University, Melbourne, Victoria, Australia | - |
dc.identifier.affiliation | Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria, Australia | - |
dc.identifier.affiliation | Department of Chemistry and Physics, La Trobe Institute for Molecular Science, Melbourne, Victoria, Australia | - |
dc.identifier.doi | 10.1080/15548627.2016.1140292 | - |
dc.identifier.pubmedid | 27046249 | - |
dc.type.austin | Journal Article | - |
dc.type.austin | Research Support, Non-U.S. Gov't | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.grantfulltext | none | - |
item.openairetype | Journal Article | - |
item.cerifentitytype | Publications | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
Appears in Collections: | Journal articles |
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