2XMR
Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor
Summary for 2XMR
| Entry DOI | 10.2210/pdb2xmr/pdb |
| Related | 2XMQ 2XMS |
| Descriptor | PROTEIN NDRG2, CALCIUM ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | signaling protein, ndrg family |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm: Q9UN36 |
| Total number of polymer chains | 3 |
| Total formula weight | 94157.51 |
| Authors | |
| 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 Cited by 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: 21247902DOI: 10.1074/JBC.M110.170803 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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