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NDRG1 participates in peripheral nerve myelination, and mutations in the <jats:italic>NDRG1<\/jats:italic> gene lead to Charcot\u2010Marie\u2010Tooth neuropathy. The 43\u2010kDa NDRG1 is considered as an inactive member of the \u03b1\/\u03b2 hydrolase superfamily. In addition to a central \u03b1\/\u03b2 hydrolase fold domain, NDRG1 consists of a short N terminus and a C\u2010terminal region with three 10\u2010residue repeats. We determined the crystal structure of the \u03b1\/\u03b2 hydrolase domain of human NDRG1 and characterised the structure and dynamics of full\u2010length NDRG1. The structure of the \u03b1\/\u03b2 hydrolase domain resembles the canonical \u03b1\/\u03b2 hydrolase fold with a central \u03b2 sheet surrounded by \u03b1 helices. Small\u2010angle X\u2010ray scattering and CD spectroscopy indicated a variable conformation for the N\u2010 and C\u2010terminal regions. NDRG1 binds to various types of lipid vesicles, and the conformation of the C\u2010terminal 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.<\/jats:p><\/jats:sec><jats:sec><jats:title>Databases<\/jats:title><jats:p>The coordinates and structure factors for the crystal structure of human NDRG1 were deposited to PDB (PDB ID: <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"https:\/\/doi.org\/10.2210\/pdb6ZMM\/pdb\">6ZMM<\/jats:ext-link>).<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.15660","type":"journal-article","created":{"date-parts":[[2020,12,11]],"date-time":"2020-12-11T07:35:37Z","timestamp":1607672137000},"page":"3507-3529","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["Crystal and solution structure of NDRG1, a membrane\u2010binding protein linked to myelination and tumour 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