Crystal and solution structure of NDRG1, a membrane‐binding protein linked to myelination and tumour suppression

N-myc downstream-regulated gene 1 (NDRG1) is a tumour suppressor involved in vesicular trafficking and stress response. NDRG1 participates peripheral nerve myelination, mutations the lead to Charcot-Marie-Tooth neuropathy. The 43-kDa considered as an inactive member of α/β hydrolase superfamily. In addition central fold domain, consists short N terminus C-terminal region with three 10-residue repeats. We determined crystal structure domain human characterised dynamics full-length NDRG1. resembles canonical β sheet surrounded by α helices. Small-angle X-ray scattering CD spectroscopy indicated variable conformation for N- regions. binds various types lipid vesicles, modulated upon interaction. Intriguingly, interacts metal ions, such nickel, but prone aggregation their presence. Our results uncover structural dynamic features NDRG1, well elucidate its interactions metals lipids, encourage studies identify putative activity Databases coordinates factors were deposited PDB (PDB ID: 6ZMM).