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dc.contributor.authorMustonen, Venla
dc.contributor.authorMuruganandam, Gopinath
dc.contributor.authorLoris, Remy
dc.contributor.authorKursula, Petri
dc.contributor.authorRuskamo, Salla
dc.date.accessioned2021-06-24T09:11:39Z
dc.date.available2021-06-24T09:11:39Z
dc.date.created2021-02-06T12:51:23Z
dc.date.issued2021
dc.identifier.issn1742-464X
dc.identifier.urihttps://hdl.handle.net/11250/2761066
dc.description.abstractN-myc downstream-regulated gene 1 (NDRG1) is a tumour suppressor involved in vesicular trafficking and stress response. NDRG1 participates in peripheral nerve myelination, and mutations in the NDRG1 gene lead to Charcot-Marie-Tooth neuropathy. The 43-kDa NDRG1 is considered as an inactive member of the α/β hydrolase superfamily. In addition to a central α/β hydrolase fold domain, NDRG1 consists of a short N terminus and a C-terminal region with three 10-residue repeats. We determined the crystal structure of the α/β hydrolase domain of human NDRG1 and characterised the structure and dynamics of full-length NDRG1. The structure of the α/β hydrolase domain resembles the canonical α/β hydrolase fold with a central β sheet surrounded by α helices. Small-angle X-ray scattering and CD spectroscopy indicated a variable conformation for the N- and C-terminal regions. NDRG1 binds to various types of lipid vesicles, and the conformation of the C-terminal region is modulated upon lipid interaction. Intriguingly, NDRG1 interacts with metal ions, such as nickel, but is prone to aggregation in their presence. Our results uncover the structural and dynamic features of NDRG1, as well as elucidate its interactions with metals and lipids, and encourage studies to identify a putative hydrolase activity of NDRG1.en_US
dc.language.isoengen_US
dc.publisherWileyen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleCrystal and solution structure of NDRG1, a membranebinding protein linked to myelination and tumour suppressionen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2020 The Authorsen_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2
dc.identifier.doi10.1111/febs.15660
dc.identifier.cristin1887274
dc.source.journalThe FEBS Journalen_US
dc.source.pagenumber3507-3529en_US
dc.identifier.citationThe FEBS Journal. 2021, 288 (11), 3507-3529.en_US
dc.source.volume288en_US
dc.source.issue11en_US


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Navngivelse 4.0 Internasjonal
Except where otherwise noted, this item's license is described as Navngivelse 4.0 Internasjonal