Tucker, J. et al. Expression of p21 proteins in Escherichia coli and stereochemistry of th nucleotide-binding site. EMBO J. 5, 1351-1358

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dc.contributor.authorTucker, J.
dc.contributor.authorSczakiel, Georg
dc.contributor.authorFeuerstein, Juergen W.
dc.contributor.authorJohn, Jasson
dc.contributor.authorGoody, Roger S.
dc.contributor.authorWittinghofer, Alfred
dc.date.accessioned2016-07-14T20:56:39Z
dc.date.available2016-07-14T20:56:39Z
dc.date.issued1986-06
dc.description.abstractv-Ha-ras encoded p21 protein (p21V), the cellular c-Ha-ras encoded protein (p21C) and its T24 mutant form p21T were produced in Escherichia coli under the control of the tac promoter. Large amounts of the authentic proteins in a soluble form can be extracted and purified without the use of denaturants or detergents. All three proteins are highly active in GDP binding, GTPase and, for p21V, autokinase activity. Inhibition of [3H]GDP binding to p21C by regio- and stereospecific phosphorothioate analogs of GDP and GTP was investigated to obtain a measure of the relative affinities of the three diphosphate and five triphosphate analogs of guanosine. p21 has a preference for the Sp isomers of GDP alpha S and GTP alpha S. It has low specificity for the Sp isomer of GTP beta S. Together with the data for GDP beta S and GTP gamma S these results are compared with those obtained for elongation factor (EF)Tu and transducin. This has enabled us to probe the structural relatedness of these proteins. We conclude that p21 seems to be more closely related to EF-Tu than to transducin.en_US
dc.identifier.citationTucker, J., Sczakiel, G., Feuerstein, J., John, J., Goody, R.S. and Wittinghofer, A., 1986. Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site. The EMBO Journal, 5(6), p.1351.en_US
dc.identifier.urihttp://hdl.handle.net/20.500.11810/3228
dc.language.isoenen_US
dc.titleTucker, J. et al. Expression of p21 proteins in Escherichia coli and stereochemistry of th nucleotide-binding site. EMBO J. 5, 1351-1358en_US
dc.typeJournal Article, Peer Revieweden_US
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