Structural and biophysical analyses of human N-MYC downstream-regulated gene 3 (NDRG3) protein
DC Field | Value | Language |
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dc.contributor.author | Kim K.R. | - |
dc.contributor.author | Kim K.A. | - |
dc.contributor.author | Park J.S. | - |
dc.contributor.author | Jang J.Y. | - |
dc.contributor.author | Choi Y. | - |
dc.contributor.author | Lee H.H. | - |
dc.contributor.author | Lee D.C. | - |
dc.contributor.author | Park K.C. | - |
dc.contributor.author | Yeom Y.I. | - |
dc.contributor.author | Kim H.-J. | - |
dc.contributor.author | Han B.W. | - |
dc.date.available | 2020-04-10T03:20:42Z | - |
dc.date.issued | 2020-01 | - |
dc.identifier.issn | 2218-273X | - |
dc.identifier.issn | 2218-273X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/38223 | - |
dc.description.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. © 2020 by the authors. Licensee MDPI, Basel, Switzerland. | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | MDPI AG | - |
dc.title | Structural and biophysical analyses of human N-MYC downstream-regulated gene 3 (NDRG3) protein | - |
dc.type | Article | - |
dc.identifier.doi | 10.3390/biom10010090 | - |
dc.identifier.bibliographicCitation | Biomolecules, v.10, no.1 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000514863200043 | - |
dc.identifier.scopusid | 2-s2.0-85077851412 | - |
dc.citation.number | 1 | - |
dc.citation.title | Biomolecules | - |
dc.citation.volume | 10 | - |
dc.type.docType | Article | - |
dc.publisher.location | 스위스 | - |
dc.subject.keywordAuthor | Crystal structure | - |
dc.subject.keywordAuthor | NDRG3 | - |
dc.subject.keywordAuthor | Unfolded helix | - |
dc.subject.keywordAuthor | α/β-hydrolase fold | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | PROLIFERATION | - |
dc.subject.keywordPlus | SERVER | - |
dc.subject.keywordPlus | METASTASIS | - |
dc.subject.keywordPlus | SUPPRESSES | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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