Crystal Structure of the Human N-Myc Downstream-regulated Gene 2 Protein Provides Insight into Its Role as a Tumor Suppressor

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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 alpha/beta-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 angstrom 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 alpha 6 in the suppression of TCF/beta-catenin signaling in the tumorigenesis of human colorectal cancer, via a molecular interaction.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
2011-04
Language
English
Article Type
Article
Keywords

COLON-CARCINOMA CELLS; BETA-CATENIN; METASTASIS SUPPRESSOR; COLORECTAL-CANCER; PROSTATE-CANCER; DOWN-REGULATION; C-MYC; NDRG2; EXPRESSION; DIFFERENTIATION

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.286, no.14, pp.12450 - 12460

ISSN
0021-9258
DOI
10.1074/jbc.M110.170803
URI
http://hdl.handle.net/10203/96830
Appears in Collection
CH-Journal Papers(저널논문)
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