Comparative modelling and immunochemical reactivity of Escherichia coli UMP kinase

Bacterial UMP kinases do not exhibit any sequence homology with other nucleoside monophosphate kinases described so far, and appear under oligomeric forms, submitted to complex regulation by nucleotides. We propose here a structural model of UMP kinase from Escherichia coli based on the conservation...

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Veröffentlicht in:	Biochemical and biophysical research communications 2002-05, Vol.294 (1), p.173-179
Hauptverfasser:	Labesse, Gilles, Bucurenci, Nadia, Douguet, Dominique, Sakamoto, Hiroshi, Landais, Stéphanie, Gagyi, Cristina, Gilles, Anne-Marie, Bârzu, Octavian
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bioinformatics Chemical Sciences Cheminformatics Computer Science Dimerization Enterococcus faecalis Escherichia coli Escherichia coli - enzymology Life Sciences Medicinal Chemistry Models, Molecular Molecular modelling Molecular Sequence Data Nucleoside-Phosphate Kinase - chemistry Pharmaceutical sciences Remote similarity Sequence Alignment Site-directed mutagenesis Structure-Activity Relationship Structure–function relationship UMP kinase
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