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CRYSTAL STRUCTURE OF HUMAN NDRG2 PROTEIN PROVIDES INSIGHT INTO ITS ROLE AS A TUMOR SUPPRESSOR
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 alpha/beta hydrolase 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 alpha/beta hydrolase superfamily of proteins, despite limited sequence similarity. Structural analysis suggests that NDRG2 is a non-enzymatic member of the alpha/beta hydrolase superfamily, since 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 alpha6 in the suppression of TCF/beta-catenin signaling in the tumorigenesis of human colorectal cancer, via a molecular interaction.
Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor., Hwang J, Kim Y, Kang HB, Jaroszewski L, Deacon A, Lee H, Choi WC, Kim KJ, Kim CH, Kang BS, Lee JO, Oh TK, Kim JW, Wilson IA, Kim MH, J Biol Chem. 2011 Jan 18. PMID:21247902
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.