6L4H
Crystal structure of human NDRG3 C30S mutant
Summary for 6L4H
| Entry DOI | 10.2210/pdb6l4h/pdb |
| Descriptor | Protein NDRG3 (1 entity in total) |
| Functional Keywords | alpha/beta-hydrolase fold, ndrg3, unfolded helix, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 165734.08 |
| Authors | |
| Primary citation | 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 Cited by 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: 31935861DOI: 10.3390/biom10010090 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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