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  Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene

Erent, M., Gonin, P., Cherfils, J., Tissier, P., Raschella, G., Giartosio, A., et al. (2001). Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene. European Journal of Biochemistry, 268(7), 1972-1981. doi:10.1046/j.1432-1327.2001.2076.doc.x.

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EurJBiochem_268_2001_1972.pdf (Any fulltext), 967KB
 
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 Creators:
Erent, Muriel1, 2, Author              
Gonin, Philippe, Author
Cherfils, Jacqueline, Author
Tissier, Pierre, Author
Raschella, Giuseppe, Author
Giartosio, Anna, Author
Agou, Fabrice, Author
Sarger, Claude, Author
Lacombe, Marie−Lise, Author
Konrad, Manfred, Author
Lascu, Ioan, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              

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Free keywords: Drnm23; hybrid; nucleoside diphosphate kinase; oligomeric proteins; protein stability
 Abstract: The human DRnm23 gene was identified by differential screening of a cDNA library obtained from chronic myeloid leukaemia-blast crisis primary cells. The over-expression of this gene inhibits differentiation and induces the apoptosis of myeloid precursor cell lines. We overproduced in bacteria a truncated form of the encoded protein lacking the first 17 N-terminal amino acids. This truncated protein was called nucleoside diphosphate (NDP) kinase CDelta. NDP kinase CDelta had similar kinetic properties to the major human NDP kinases A and B, but was significantly more stable to denaturation by urea and heat. Analysis of denaturation by urea, using size exclusion chromatography, indicated unfolding without the dissociation of subunits, whereas renaturation occurred via a folded monomer. The stability of the protein depended primarily on subunit interactions. Homology modelling of the structure of NDP kinase CDelta, based on the crystal structure of NDP kinase B, indicated that NDP kinase CDelta had several additional stabilizing interactions. The overall structure of the two enzymes appears to be identical because NDP kinase CDelta readily formed mixed hexamers with NDP kinase A. It is possible that mixed hexamers can be observed in vivo.

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Language(s): eng - English
 Dates: 2001-02-012000-12-042001-02-022001-12-202001-04
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 268 (7) Sequence Number: - Start / End Page: 1972 - 1981 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040