6L4B

Crystal structure of human WT NDRG3

6L4B の概要

• エントリーDOI: 10.2210/pdb6l4b/pdb
• 分子名称: Protein NDRG3 (2 entities in total)
• 機能のキーワード: alpha/beta-hydrolase fold, ndrg3, unfolded helix, signaling protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 248697.52

構造登録者

Kim, K.R.,Han, B.W. (登録日: 2019-10-16, 公開日: 2020-08-26, 最終更新日: 2024-10-23)

主引用文献

Kim, K.R.,Kim, K.A.,Park, J.S.,Jang, J.Y.,Choi, Y.,Lee, H.H.,Lee, D.C.,Park, K.C.,Yeom, Y.I.,Kim, H.J.,Han, B.W.
Structural and Biophysical Analyses of Human N-Myc Downstream-Regulated Gene 3 (NDRG3) Protein.
Biomolecules, 10:-, 2020

PubMed Abstract: The N-Myc downstream-regulated gene (NDRG) family belongs to the α/β-hydrolase fold and is known to exert various physiologic functions in cell proliferation, differentiation, and hypoxia-induced cancer metabolism. In particular, NDRG3 is closely related to proliferation and migration of prostate cancer cells, and recent studies reported its implication in lactate-triggered hypoxia responses or tumorigenesis. However, the underlying mechanism for the functions of NDRG3 remains unclear. Here, we report the crystal structure of human NDRG3 at 2.2 Å resolution, with six molecules in an asymmetric unit. While NDRG3 adopts the α/β-hydrolase fold, complete substitution of the canonical catalytic triad residues to non-reactive residues and steric hindrance around the pseudo-active site seem to disable the α/β-hydrolase activity. While NDRG3 shares a high similarity to NDRG2 in terms of amino acid sequence and structure, NDRG3 exhibited remarkable structural differences in a flexible loop corresponding to helix α6 of NDRG2 that is responsible for tumor suppression. Thus, this flexible loop region seems to play a distinct role in oncogenic progression induced by NDRG3. Collectively, our studies could provide structural and biophysical insights into the molecular characteristics of NDRG3.

PubMed: 31935861
DOI: 10.3390/biom10010090

実験手法

X-RAY DIFFRACTION (2.2 Å)