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- Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor
- Jungwon Hwang; Y Kim; Ho-Bum Kang; L Jaroszewski; A M Deacon; H Lee; W C Choi; K J Kim; C H Kim; B S Kang; J O Lee; Tae Kwang Oh; Jae Wha Kim; I A Wilson; Myung Hee Kim
- Bibliographic Citation
- Journal of Biological Chemistry, vol. 286, no. 14, pp. 12450-12460
- Publication Year
- Considerable attention has recently been paid to the N-Myc downstream-regulated gene (NDRG) family because of its potential as a tumor suppressor in many human cancers. Primary amino acid sequence information suggests that the NDRG family proteins may belong to the α/β-hydrolase (ABH) superfamily; however, their functional role has not yet been determined. Here, we present the crystal structures of the human and mouse NDRG2 proteins determined at 2.0 and 1.7 Å resolution, respectively. Both NDRG2 proteins show remarkable structural similarity to the ABH superfamily, despite limited sequence similarity. Structural analysis suggests that NDRG2 is a nonenzymatic member of the ABH superfamily, because it lacks the catalytic signature residues and has an occluded substrate-binding site. Several conserved structural features suggest NDRG may be involved in molecular interactions. Mutagenesis data based on the structural analysis support a crucial role for helix α6 in the suppression of TCF/β-catenin signaling in the tumorigenesis of human colorectal cancer, via a molecular interaction.
- Amer Soc Biochemistry Molecular Biology Inc
- Appears in Collections:
- Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomaterials Research > Cell Factory Research Center > 1. Journal Articles
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