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Crystal and solution structure of NDRG1, a membrane‐binding protein linked to myelination and tumour suppression
Author(s) -
Mustonen Venla,
Muruganandam Gopinath,
Loris Remy,
Kursula Petri,
Ruskamo Salla
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15660
Subject(s) - protein data bank (rcsb pdb) , hydrolase , chemistry , protein structure , crystallography , gene , crystal structure , biology , biochemistry , enzyme
N‐myc downstream‐regulated gene 1 (NDRG1) plays a role in the maintenance of the myelin sheaths in peripheral nerves. The crystal structure of the α/β hydrolase domain of human NDRG1 resembles the canonical α/β hydrolase fold. The N and C termini of NDRG1 are flexible and obtain variable conformations. NDRG1 binds to metal ions and lipid vesicles, and the conformation of the C‐terminal region is modulated upon lipid interaction.