2XMS

Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor

Summary for 2XMS

• Entry DOI: 10.2210/pdb2xms/pdb
• Related: 2XMQ 2XMR
• Descriptor: PROTEIN NDRG2, CHLORIDE ION, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: signaling protein, ndrg family
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: Q9UN36
• Total number of polymer chains: 1
• Total formula weight: 31579.15

Authors

Hwang, J.,Kim, Y.,Lee, H.,Kim, M.H. (deposition date: 2010-07-29, release date: 2011-01-19, Last modification date: 2023-12-20)

Primary citation

Hwang, J.,Kim, Y.,Kang, H.B.,Jaroszewski, L.,Deacon, A.,Lee, H.,Choi, W.C.,Kim, K.J.,Kim, C.H.,Kang, B.S.,Lee, J.O.,Oh, T.K.,Kim, J.W.,Wilson, I.A.,Kim, M.H.
Crystal Structure of Human Ndrg2 Protein Provides Insight Into its Role as a Tumor Suppressor.
J.Biol.Chem., 286:12450-, 2011

PubMed Abstract: 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.

PubMed: 21247902
DOI: 10.1074/JBC.M110.170803

Experimental method

X-RAY DIFFRACTION (2.15 Å)