Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 14, Pages 12450-12460Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.170803
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Funding
- Ministry of Education, Science, and Technology
- Ministry for Health, Welfare and Family Affairs, Republic of Korea [A090509]
- National Institutes of Health, NIGMS Protein Structure Initiative [U54 GM074898]
- National Science Foundation
- University of California and Henry Wheeler
- Department of Energy, Office of Biological and Environmental Research
- National Institutes of Health (NCRR Biomedical Technology Program and NIGMS)
- Office of Science, Office of Basic Energy Sciences, of the United States Department of Energy [DE-AC02-05CH11231]
- Korea Health Promotion Institute [A090509] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2008-0060543] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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.
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