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A preliminary X-ray study of human nucleoside diphosphate kinase A under oxidative conditions

Title
A preliminary X-ray study of human nucleoside diphosphate kinase A under oxidative conditions
Authors
Kim M.-S.Jeong J.Lee K.-J.Shin D.H.
Ewha Authors
이공주신동해
SCOPUS Author ID
이공주scopus; 신동해scopus
Issue Date
2010
Journal Title
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
ISSN
1744-3091JCR Link
Citation
vol. 66, no. 11, pp. 1490 - 1492
Indexed
SCOPUS WOS scopus
Abstract
Nucleoside diphosphate kinase (NDPK) catalyzes transfer of the - phosphoryl group from a nucleoside triphosphate (NTP) to a nucleoside diphosphate. The high-energy phosphate for this reaction is usually supplied by ATP. NDPK plays a primary role not only in maintaining cellular pools of all NTPs but also in the regulation of important cellular processes. NDPK-A (or Nm23-H1), one of eight human NDPKs, acts as a metastasis suppressor for some tumour types. A recent study showed that homohexameric human NDPK-A is regulated in response to oxidative stress. The activity of NDPK-A is reduced, with a concomitant increase in the population of dimeric NDPK-A, under oxidative conditions. In this study, human NDPK-A has been crystallized under oxidative conditions and X-ray data have been collected to 2.80 Å resolution using synchrotron radiation. The crystal belonged to the primitive cubic space group P213, with unit-cell parameters a = b = c = 106.8 Å. There is one NDPK-A dimer in the asymmetric unit. The preliminary electron-density map shows a large conformational change of the C-terminal domain of NDPK-A induced by a novel disulfide bond that is formed under oxidative conditions. © 2010 International Union of Crystallography All rights reserved.
DOI
10.1107/S1744309110036067
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약학대학 > 약학과 > Journal papers
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