2XMR
Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor
2XMR の概要
エントリーDOI | 10.2210/pdb2xmr/pdb |
関連するPDBエントリー | 2XMQ 2XMS |
分子名称 | PROTEIN NDRG2, CALCIUM ION, ACETATE ION, ... (5 entities in total) |
機能のキーワード | signaling protein, ndrg family |
由来する生物種 | HOMO SAPIENS (HUMAN) |
細胞内の位置 | Cytoplasm: Q9UN36 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 94157.51 |
構造登録者 | |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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