Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2013.01.039
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dc.titleALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its β-sandwich fold into lipid-interacting helical conformations
dc.contributor.authorQin, H.
dc.contributor.authorWang, W.
dc.contributor.authorSong, J.
dc.date.accessioned2014-10-27T08:21:18Z
dc.date.available2014-10-27T08:21:18Z
dc.date.issued2013-02-15
dc.identifier.citationQin, H., Wang, W., Song, J. (2013-02-15). ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its β-sandwich fold into lipid-interacting helical conformations. Biochemical and Biophysical Research Communications 431 (3) : 398-403. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2013.01.039
dc.identifier.issn0006291X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100037
dc.description.abstractP56S mutation on VAPB MSP domain causes a familial ALS, characteristic of severe aggregation both in vivo and in vitro. We previously showed that P56S rendered the MSP domain to be predominantly disordered in water. Unexpectedly, here we reveal that P56S-MSP transforms into a highly helical conformation in a membrane environment. This chameleon transformation is shared by a splicing variant VAPB-3 with a truncated MSP domain, which is also highly disordered and buffer insoluble as demonstrated here by NMR. Our discovery provides a mechanism for ALS-causing VAPB mutants/variants to gain novel functions such as to mediate ER structure before significant accumulation of aggregates occurs. © 2013 Elsevier Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bbrc.2013.01.039
dc.sourceScopus
dc.subjectAmyotrophic lateral sclerosis (ALS)
dc.subjectChameleon transformation
dc.subjectDodecylphosphocholine (DPC)
dc.subjectNMR spectroscopy
dc.subjectProtein aggregation
dc.subjectVAPB
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.bbrc.2013.01.039
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume431
dc.description.issue3
dc.description.page398-403
dc.description.codenBBRCA
dc.identifier.isiut000315842800006
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